PSB1_YEAST
ID PSB1_YEAST Reviewed; 215 AA.
AC P38624; D6VWH4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Proteasome subunit beta type-1;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit PRE3;
DE AltName: Full=Multicatalytic endopeptidase complex subunit PRE3;
DE AltName: Full=Proteasome component PRE3;
DE AltName: Full=Proteinase YSCE subunit PRE3;
DE Flags: Precursor;
GN Name=PRE3; OrderedLocusNames=YJL001W; ORFNames=J1407;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7907993; DOI=10.1016/0014-5793(94)80455-9;
RA Enenkel C., Lehmann H., Kipper J., Gueckel R., Hilt W., Wolf D.H.;
RT "PRE3, highly homologous to the human major histocompatibility complex-
RT linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary
RT for the peptidylglutamyl-peptide hydrolyzing activity.";
RL FEBS Lett. 341:193-196(1994).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=7781614; DOI=10.1002/j.1460-2075.1995.tb07260.x;
RA Chen P., Hochstrasser M.;
RT "Biogenesis, structure and function of the yeast 20S proteasome.";
RL EMBO J. 14:2620-2630(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-215 OF COMPLEX WITH THE 20S
RP PROTEASOME, PROTEOLYTIC PROCESSING, AND ACTIVE SITE.
RX PubMed=9087403; DOI=10.1038/386463a0;
RA Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D.,
RA Huber R.;
RT "Structure of 20S proteasome from yeast at 2.4-A resolution.";
RL Nature 386:463-471(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE 20S
RP PROTEASOME AND A 11S REGULATORY COMPLEX.
RX PubMed=11081519; DOI=10.1038/35040607;
RA Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C.,
RA Hill C.P.;
RT "Structural basis for the activation of 20S proteasomes by 11S
RT regulators.";
RL Nature 408:115-120(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE 20S
RP PROTEASOME.
RX PubMed=11062564; DOI=10.1038/80992;
RA Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R.,
RA Glickman M.H., Finley D.;
RT "A gated channel into the proteasome core particle.";
RL Nat. Struct. Biol. 7:1062-1067(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE 20S
RP PROTEASOME AND A TMC-95-BASED INHIBITOR.
RX PubMed=16793518; DOI=10.1016/j.chembiol.2006.04.005;
RA Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.;
RT "TMC-95-based inhibitor design provides evidence for the catalytic
RT versatility of the proteasome.";
RL Chem. Biol. 13:607-614(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE 20S
RP PROTEASOME AND SALINOSPORAMIDE.
RX PubMed=16608349; DOI=10.1021/ja058320b;
RA Groll M., Huber R., Potts B.C.M.;
RT "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in
RT complex with the 20S proteasome reveal important consequences of beta-
RT lactone ring opening and a mechanism for irreversible binding.";
RL J. Am. Chem. Soc. 128:5136-5141(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE 20S
RP PROTEASOME AND BORTEZOMIB.
RX PubMed=16531229; DOI=10.1016/j.str.2005.11.019;
RA Groll M., Berkers C.R., Ploegh H.L., Ovaa H.;
RT "Crystal structure of the boronic acid-based proteasome inhibitor
RT bortezomib in complex with the yeast 20S proteasome.";
RL Structure 14:451-456(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-215 IN COMPLEX WITH THE
RP PROTEASOME.
RX PubMed=20227375; DOI=10.1016/j.molcel.2010.02.002;
RA Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.;
RT "Structure of a Blm10 complex reveals common mechanisms for proteasome
RT binding and gate opening.";
RL Mol. Cell 37:728-735(2010).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
RX PubMed=22927375; DOI=10.1073/pnas.1213333109;
RA Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E.,
RA Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.;
RT "Near-atomic resolution structural model of the yeast 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012).
CC -!- FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the
CC cytoplasm and in the nucleus. It is essential for the regulated
CC turnover of proteins and for the removal of misfolded proteins. The
CC proteasome is a multicatalytic proteinase complex that is characterized
CC by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu
CC adjacent to the leaving group at neutral or slightly basic pH. It has
CC an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for
CC the peptidyl-glutamyl-peptide-hydrolyzing activity.
CC -!- FUNCTION: This subunit is necessary for the peptidylglutamyl-peptide
CC hydrolyzing activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000269|PubMed:20227375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: The side chain of Thr-20 acts as nucleophile, and the N-
CC terminal amino group acts as proton acceptor.
CC -!- MISCELLANEOUS: Present with 7250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA60921.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X78991; CAA55591.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49276; CAA89290.1; -; Genomic_DNA.
DR EMBL; Z49277; CAA89292.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60921.1; ALT_INIT; Genomic_DNA.
DR EMBL; X86020; CAA60015.1; -; mRNA.
DR EMBL; S78566; AAB34629.1; -; mRNA.
DR EMBL; BK006943; DAA08790.1; -; Genomic_DNA.
DR PIR; S61337; S61337.
DR RefSeq; NP_012533.1; NM_001181435.1.
DR PDB; 1FNT; X-ray; 3.20 A; H/V=20-215.
DR PDB; 1G0U; X-ray; 2.40 A; 2/N=20-215.
DR PDB; 1G65; X-ray; 2.25 A; 2/N=20-215.
DR PDB; 1JD2; X-ray; 3.00 A; N/U=20-215.
DR PDB; 1RYP; X-ray; 1.90 A; H/V=11-215.
DR PDB; 1Z7Q; X-ray; 3.22 A; H/V=20-215.
DR PDB; 2F16; X-ray; 2.80 A; 2/N=20-215.
DR PDB; 2FAK; X-ray; 2.80 A; 2/N=20-215.
DR PDB; 2GPL; X-ray; 2.81 A; 2/N=20-215.
DR PDB; 2ZCY; X-ray; 2.90 A; 1/N=20-215.
DR PDB; 3BDM; X-ray; 2.70 A; 1/N=20-215.
DR PDB; 3D29; X-ray; 2.60 A; 2/N=20-215.
DR PDB; 3DY3; X-ray; 2.81 A; 2/N=20-215.
DR PDB; 3DY4; X-ray; 2.80 A; 2/N=20-215.
DR PDB; 3E47; X-ray; 3.00 A; 2/N=20-215.
DR PDB; 3GPJ; X-ray; 2.70 A; 2/N=20-215.
DR PDB; 3GPT; X-ray; 2.41 A; 2/N=20-215.
DR PDB; 3GPW; X-ray; 2.50 A; 2/N=20-215.
DR PDB; 3HYE; X-ray; 2.50 A; 2/N=20-215.
DR PDB; 3JCO; EM; 4.80 A; 3/h=1-215.
DR PDB; 3JCP; EM; 4.60 A; 3/h=1-215.
DR PDB; 3MG0; X-ray; 2.68 A; 2/N=20-215.
DR PDB; 3MG4; X-ray; 3.11 A; 2/N=20-215.
DR PDB; 3MG6; X-ray; 2.60 A; 2/N=20-215.
DR PDB; 3MG7; X-ray; 2.78 A; 2/N=20-215.
DR PDB; 3MG8; X-ray; 2.59 A; 2/N=20-215.
DR PDB; 3NZJ; X-ray; 2.40 A; 2/N=1-215.
DR PDB; 3NZW; X-ray; 2.50 A; 2/N=1-215.
DR PDB; 3NZX; X-ray; 2.70 A; 2/N=1-215.
DR PDB; 3OEU; X-ray; 2.60 A; 2/N=20-215.
DR PDB; 3OEV; X-ray; 2.85 A; 2/N=20-215.
DR PDB; 3OKJ; X-ray; 2.70 A; 2/N=20-215.
DR PDB; 3SDI; X-ray; 2.65 A; 2/N=20-215.
DR PDB; 3SDK; X-ray; 2.70 A; 2/N=20-215.
DR PDB; 3SHJ; X-ray; 2.80 A; 2/N=20-215.
DR PDB; 3TDD; X-ray; 2.70 A; 2/N=20-215.
DR PDB; 3UN4; X-ray; 3.40 A; N/b=20-215.
DR PDB; 3UN8; X-ray; 2.70 A; N/b=20-215.
DR PDB; 3WXR; X-ray; 3.15 A; H/V=1-215.
DR PDB; 4CR2; EM; 7.70 A; 1=1-215.
DR PDB; 4CR3; EM; 9.30 A; 1=1-215.
DR PDB; 4CR4; EM; 8.80 A; 1=1-215.
DR PDB; 4EU2; X-ray; 2.51 A; H/V=20-215.
DR PDB; 4FZC; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4FZG; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4G4S; X-ray; 2.49 A; H=20-215.
DR PDB; 4GK7; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4HNP; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4HRC; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4HRD; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4INR; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4INT; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4INU; X-ray; 3.10 A; N/b=20-215.
DR PDB; 4J70; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4JSQ; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4JSU; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4JT0; X-ray; 3.10 A; N/b=20-215.
DR PDB; 4LQI; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4LTC; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4NNN; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4NNW; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4NO1; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4NO6; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4NO8; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4NO9; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4Q1S; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QBY; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QLQ; X-ray; 2.40 A; N/b=20-215.
DR PDB; 4QLS; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QLT; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QLU; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QLV; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QUX; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QUY; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QV0; X-ray; 3.10 A; N/b=20-215.
DR PDB; 4QV1; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4QV3; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QV4; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4QV5; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4QV6; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QV7; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QV8; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QV9; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QVL; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QVM; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QVN; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QVP; X-ray; 2.30 A; N/b=20-215.
DR PDB; 4QVQ; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QVV; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QVW; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QVY; X-ray; 2.51 A; N/b=20-215.
DR PDB; 4QW0; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QW1; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QW3; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QW4; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QW5; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QW6; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QW7; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4QWF; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QWG; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QWI; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QWJ; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QWK; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QWL; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QWR; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QWS; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QWU; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QWX; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QXJ; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QZ0; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QZ1; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QZ2; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4QZ3; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QZ4; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QZ5; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QZ6; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4QZ7; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4QZW; X-ray; 3.00 A; N/b=20-215.
DR PDB; 4QZX; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4QZZ; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4R00; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4R02; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4R17; X-ray; 2.10 A; N/b=20-215.
DR PDB; 4R18; X-ray; 2.40 A; N/b=20-215.
DR PDB; 4RUR; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4V7O; X-ray; 3.00 A; AB/AD/BH/BV=21-215.
DR PDB; 4X6Z; X-ray; 2.70 A; H/V=1-215.
DR PDB; 4Y69; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4Y6A; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y6V; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y6Z; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y70; X-ray; 2.40 A; N/b=20-215.
DR PDB; 4Y74; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y75; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y77; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4Y78; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y7W; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4Y7X; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y7Y; X-ray; 2.40 A; N/b=20-215.
DR PDB; 4Y80; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4Y81; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y82; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y84; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y8G; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y8H; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4Y8I; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y8J; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y8K; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y8L; X-ray; 2.40 A; N/b=20-215.
DR PDB; 4Y8M; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y8N; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y8O; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y8P; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y8Q; X-ray; 2.60 A; N/b=20-215.
DR PDB; 4Y8R; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y8S; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y8T; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Y8U; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4Y9Y; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4Y9Z; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4YA0; X-ray; 2.80 A; N/b=20-215.
DR PDB; 4YA1; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4YA2; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4YA3; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4YA4; X-ray; 2.90 A; N/b=20-215.
DR PDB; 4YA5; X-ray; 2.50 A; N/b=20-215.
DR PDB; 4YA7; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4YA9; X-ray; 2.70 A; N/b=20-215.
DR PDB; 4Z1L; X-ray; 3.00 A; N/b=20-215.
DR PDB; 5A5B; EM; 9.50 A; 1=1-215.
DR PDB; 5AHJ; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5BOU; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5BXL; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5BXN; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5CGF; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5CGG; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5CGH; X-ray; 2.50 A; N/b=20-215.
DR PDB; 5CGI; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5CZ4; X-ray; 2.30 A; N/b=20-215.
DR PDB; 5CZ5; X-ray; 2.80 A; N/b=10-215.
DR PDB; 5CZ6; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5CZ7; X-ray; 2.50 A; N/b=20-215.
DR PDB; 5CZ8; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5CZ9; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5CZA; X-ray; 2.50 A; N/b=20-215.
DR PDB; 5D0S; X-ray; 2.50 A; N/b=20-215.
DR PDB; 5D0T; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5D0V; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5D0W; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5D0X; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5D0Z; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5DKI; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5DKJ; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5FG7; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5FG9; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5FGA; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5FGD; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5FGE; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5FGF; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5FGG; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5FGH; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5FGI; X-ray; 2.90 A; N/b=3-215.
DR PDB; 5FHS; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5JHR; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5JHS; X-ray; 3.00 A; N/b=20-215.
DR PDB; 5L52; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L54; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L55; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5A; X-ray; 2.40 A; N/b=20-215.
DR PDB; 5L5B; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L5D; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L5E; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5F; X-ray; 2.50 A; N/b=20-215.
DR PDB; 5L5H; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5L5I; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5J; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5O; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5L5P; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L5Q; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L5R; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5S; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5L5T; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5U; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5L5V; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L5W; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L5X; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L5Y; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L5Z; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L60; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L61; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L62; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L63; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L64; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L65; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5L66; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L67; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5L68; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L69; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5L6A; X-ray; 2.80 A; N/b=20-215.
DR PDB; 5L6B; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5L6C; X-ray; 2.60 A; N/b=20-215.
DR PDB; 5LAI; X-ray; 2.50 A; N/b=20-215.
DR PDB; 5LAJ; X-ray; 2.90 A; N/b=20-215.
DR PDB; 5LTT; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5M2B; X-ray; 2.70 A; N/b=20-215.
DR PDB; 5MP9; EM; 4.10 A; 1/h=1-215.
DR PDB; 5MPA; EM; 4.50 A; 1/h=1-215.
DR PDB; 5MPB; EM; 7.80 A; 1/h=1-215.
DR PDB; 5MPC; EM; 7.70 A; 1/h=1-215.
DR PDB; 5NIF; X-ray; 3.00 A; H/V=1-215.
DR PDB; 5WVI; EM; 6.30 A; 1/b=1-215.
DR PDB; 5WVK; EM; 4.20 A; 1/b=1-215.
DR PDB; 6EF3; EM; 4.17 A; 1=1-215.
DR PDB; 6FVT; EM; 4.10 A; 1/h=20-215.
DR PDB; 6FVU; EM; 4.50 A; 1/h=20-215.
DR PDB; 6FVV; EM; 5.40 A; 1/h=20-215.
DR PDB; 6FVW; EM; 4.50 A; 1/h=20-215.
DR PDB; 6FVX; EM; 4.90 A; 1/h=20-215.
DR PDB; 6FVY; EM; 6.10 A; 1/h=20-215.
DR PDB; 6G7F; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6G8M; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6G8N; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6GOP; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6H39; X-ray; 2.50 A; N/b=20-215.
DR PDB; 6HTB; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HTC; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HTD; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HTP; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HTR; X-ray; 2.60 A; N/b=20-215.
DR PDB; 6HUB; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6HUC; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HUQ; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HUU; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HUV; X-ray; 3.10 A; N/b=20-215.
DR PDB; 6HV3; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HV4; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HV5; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HV7; X-ray; 3.40 A; N/b=20-215.
DR PDB; 6HVA; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6HVR; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HVS; X-ray; 3.10 A; N/b=20-215.
DR PDB; 6HVT; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6HVU; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6HVV; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HVW; X-ray; 3.00 A; N/b=20-215.
DR PDB; 6HVX; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HVY; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HW0; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HW3; X-ray; 2.60 A; N/b=20-215.
DR PDB; 6HW4; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6HW5; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6HW6; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HW7; X-ray; 2.70 A; N/b=20-215.
DR PDB; 6HW8; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HW9; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HWA; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HWB; X-ray; 2.60 A; N/b=20-215.
DR PDB; 6HWC; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HWD; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6HWE; X-ray; 2.30 A; N/b=20-215.
DR PDB; 6HWF; X-ray; 2.50 A; N/b=20-215.
DR PDB; 6J2C; EM; 7.00 A; 1/b=1-215.
DR PDB; 6J2N; EM; 7.50 A; 1/b=1-215.
DR PDB; 6J2Q; EM; 3.80 A; 1/b=1-215.
DR PDB; 6J2X; EM; 3.80 A; 1/b=1-215.
DR PDB; 6J30; EM; 4.50 A; 1/b=1-215.
DR PDB; 6ZOU; X-ray; 2.90 A; N/b=20-215.
DR PDB; 6ZP6; X-ray; 2.80 A; N/b=20-215.
DR PDB; 6ZP8; X-ray; 3.00 A; N/b=20-215.
DR PDB; 7LS5; EM; 2.74 A; H/V=1-215.
DR PDB; 7QO3; EM; 6.10 A; 1/h=1-215.
DR PDB; 7QO5; EM; 6.00 A; 1/h=1-215.
DR PDBsum; 1FNT; -.
DR PDBsum; 1G0U; -.
DR PDBsum; 1G65; -.
DR PDBsum; 1JD2; -.
DR PDBsum; 1RYP; -.
DR PDBsum; 1Z7Q; -.
DR PDBsum; 2F16; -.
DR PDBsum; 2FAK; -.
DR PDBsum; 2GPL; -.
DR PDBsum; 2ZCY; -.
DR PDBsum; 3BDM; -.
DR PDBsum; 3D29; -.
DR PDBsum; 3DY3; -.
DR PDBsum; 3DY4; -.
DR PDBsum; 3E47; -.
DR PDBsum; 3GPJ; -.
DR PDBsum; 3GPT; -.
DR PDBsum; 3GPW; -.
DR PDBsum; 3HYE; -.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 3MG0; -.
DR PDBsum; 3MG4; -.
DR PDBsum; 3MG6; -.
DR PDBsum; 3MG7; -.
DR PDBsum; 3MG8; -.
DR PDBsum; 3NZJ; -.
DR PDBsum; 3NZW; -.
DR PDBsum; 3NZX; -.
DR PDBsum; 3OEU; -.
DR PDBsum; 3OEV; -.
DR PDBsum; 3OKJ; -.
DR PDBsum; 3SDI; -.
DR PDBsum; 3SDK; -.
DR PDBsum; 3SHJ; -.
DR PDBsum; 3TDD; -.
DR PDBsum; 3UN4; -.
DR PDBsum; 3UN8; -.
DR PDBsum; 3WXR; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 4EU2; -.
DR PDBsum; 4FZC; -.
DR PDBsum; 4FZG; -.
DR PDBsum; 4G4S; -.
DR PDBsum; 4GK7; -.
DR PDBsum; 4HNP; -.
DR PDBsum; 4HRC; -.
DR PDBsum; 4HRD; -.
DR PDBsum; 4INR; -.
DR PDBsum; 4INT; -.
DR PDBsum; 4INU; -.
DR PDBsum; 4J70; -.
DR PDBsum; 4JSQ; -.
DR PDBsum; 4JSU; -.
DR PDBsum; 4JT0; -.
DR PDBsum; 4LQI; -.
DR PDBsum; 4LTC; -.
DR PDBsum; 4NNN; -.
DR PDBsum; 4NNW; -.
DR PDBsum; 4NO1; -.
DR PDBsum; 4NO6; -.
DR PDBsum; 4NO8; -.
DR PDBsum; 4NO9; -.
DR PDBsum; 4Q1S; -.
DR PDBsum; 4QBY; -.
DR PDBsum; 4QLQ; -.
DR PDBsum; 4QLS; -.
DR PDBsum; 4QLT; -.
DR PDBsum; 4QLU; -.
DR PDBsum; 4QLV; -.
DR PDBsum; 4QUX; -.
DR PDBsum; 4QUY; -.
DR PDBsum; 4QV0; -.
DR PDBsum; 4QV1; -.
DR PDBsum; 4QV3; -.
DR PDBsum; 4QV4; -.
DR PDBsum; 4QV5; -.
DR PDBsum; 4QV6; -.
DR PDBsum; 4QV7; -.
DR PDBsum; 4QV8; -.
DR PDBsum; 4QV9; -.
DR PDBsum; 4QVL; -.
DR PDBsum; 4QVM; -.
DR PDBsum; 4QVN; -.
DR PDBsum; 4QVP; -.
DR PDBsum; 4QVQ; -.
DR PDBsum; 4QVV; -.
DR PDBsum; 4QVW; -.
DR PDBsum; 4QVY; -.
DR PDBsum; 4QW0; -.
DR PDBsum; 4QW1; -.
DR PDBsum; 4QW3; -.
DR PDBsum; 4QW4; -.
DR PDBsum; 4QW5; -.
DR PDBsum; 4QW6; -.
DR PDBsum; 4QW7; -.
DR PDBsum; 4QWF; -.
DR PDBsum; 4QWG; -.
DR PDBsum; 4QWI; -.
DR PDBsum; 4QWJ; -.
DR PDBsum; 4QWK; -.
DR PDBsum; 4QWL; -.
DR PDBsum; 4QWR; -.
DR PDBsum; 4QWS; -.
DR PDBsum; 4QWU; -.
DR PDBsum; 4QWX; -.
DR PDBsum; 4QXJ; -.
DR PDBsum; 4QZ0; -.
DR PDBsum; 4QZ1; -.
DR PDBsum; 4QZ2; -.
DR PDBsum; 4QZ3; -.
DR PDBsum; 4QZ4; -.
DR PDBsum; 4QZ5; -.
DR PDBsum; 4QZ6; -.
DR PDBsum; 4QZ7; -.
DR PDBsum; 4QZW; -.
DR PDBsum; 4QZX; -.
DR PDBsum; 4QZZ; -.
DR PDBsum; 4R00; -.
DR PDBsum; 4R02; -.
DR PDBsum; 4R17; -.
DR PDBsum; 4R18; -.
DR PDBsum; 4RUR; -.
DR PDBsum; 4V7O; -.
DR PDBsum; 4X6Z; -.
DR PDBsum; 4Y69; -.
DR PDBsum; 4Y6A; -.
DR PDBsum; 4Y6V; -.
DR PDBsum; 4Y6Z; -.
DR PDBsum; 4Y70; -.
DR PDBsum; 4Y74; -.
DR PDBsum; 4Y75; -.
DR PDBsum; 4Y77; -.
DR PDBsum; 4Y78; -.
DR PDBsum; 4Y7W; -.
DR PDBsum; 4Y7X; -.
DR PDBsum; 4Y7Y; -.
DR PDBsum; 4Y80; -.
DR PDBsum; 4Y81; -.
DR PDBsum; 4Y82; -.
DR PDBsum; 4Y84; -.
DR PDBsum; 4Y8G; -.
DR PDBsum; 4Y8H; -.
DR PDBsum; 4Y8I; -.
DR PDBsum; 4Y8J; -.
DR PDBsum; 4Y8K; -.
DR PDBsum; 4Y8L; -.
DR PDBsum; 4Y8M; -.
DR PDBsum; 4Y8N; -.
DR PDBsum; 4Y8O; -.
DR PDBsum; 4Y8P; -.
DR PDBsum; 4Y8Q; -.
DR PDBsum; 4Y8R; -.
DR PDBsum; 4Y8S; -.
DR PDBsum; 4Y8T; -.
DR PDBsum; 4Y8U; -.
DR PDBsum; 4Y9Y; -.
DR PDBsum; 4Y9Z; -.
DR PDBsum; 4YA0; -.
DR PDBsum; 4YA1; -.
DR PDBsum; 4YA2; -.
DR PDBsum; 4YA3; -.
DR PDBsum; 4YA4; -.
DR PDBsum; 4YA5; -.
DR PDBsum; 4YA7; -.
DR PDBsum; 4YA9; -.
DR PDBsum; 4Z1L; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5AHJ; -.
DR PDBsum; 5BOU; -.
DR PDBsum; 5BXL; -.
DR PDBsum; 5BXN; -.
DR PDBsum; 5CGF; -.
DR PDBsum; 5CGG; -.
DR PDBsum; 5CGH; -.
DR PDBsum; 5CGI; -.
DR PDBsum; 5CZ4; -.
DR PDBsum; 5CZ5; -.
DR PDBsum; 5CZ6; -.
DR PDBsum; 5CZ7; -.
DR PDBsum; 5CZ8; -.
DR PDBsum; 5CZ9; -.
DR PDBsum; 5CZA; -.
DR PDBsum; 5D0S; -.
DR PDBsum; 5D0T; -.
DR PDBsum; 5D0V; -.
DR PDBsum; 5D0W; -.
DR PDBsum; 5D0X; -.
DR PDBsum; 5D0Z; -.
DR PDBsum; 5DKI; -.
DR PDBsum; 5DKJ; -.
DR PDBsum; 5FG7; -.
DR PDBsum; 5FG9; -.
DR PDBsum; 5FGA; -.
DR PDBsum; 5FGD; -.
DR PDBsum; 5FGE; -.
DR PDBsum; 5FGF; -.
DR PDBsum; 5FGG; -.
DR PDBsum; 5FGH; -.
DR PDBsum; 5FGI; -.
DR PDBsum; 5FHS; -.
DR PDBsum; 5JHR; -.
DR PDBsum; 5JHS; -.
DR PDBsum; 5L52; -.
DR PDBsum; 5L54; -.
DR PDBsum; 5L55; -.
DR PDBsum; 5L5A; -.
DR PDBsum; 5L5B; -.
DR PDBsum; 5L5D; -.
DR PDBsum; 5L5E; -.
DR PDBsum; 5L5F; -.
DR PDBsum; 5L5H; -.
DR PDBsum; 5L5I; -.
DR PDBsum; 5L5J; -.
DR PDBsum; 5L5O; -.
DR PDBsum; 5L5P; -.
DR PDBsum; 5L5Q; -.
DR PDBsum; 5L5R; -.
DR PDBsum; 5L5S; -.
DR PDBsum; 5L5T; -.
DR PDBsum; 5L5U; -.
DR PDBsum; 5L5V; -.
DR PDBsum; 5L5W; -.
DR PDBsum; 5L5X; -.
DR PDBsum; 5L5Y; -.
DR PDBsum; 5L5Z; -.
DR PDBsum; 5L60; -.
DR PDBsum; 5L61; -.
DR PDBsum; 5L62; -.
DR PDBsum; 5L63; -.
DR PDBsum; 5L64; -.
DR PDBsum; 5L65; -.
DR PDBsum; 5L66; -.
DR PDBsum; 5L67; -.
DR PDBsum; 5L68; -.
DR PDBsum; 5L69; -.
DR PDBsum; 5L6A; -.
DR PDBsum; 5L6B; -.
DR PDBsum; 5L6C; -.
DR PDBsum; 5LAI; -.
DR PDBsum; 5LAJ; -.
DR PDBsum; 5LTT; -.
DR PDBsum; 5M2B; -.
DR PDBsum; 5MP9; -.
DR PDBsum; 5MPA; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5NIF; -.
DR PDBsum; 5WVI; -.
DR PDBsum; 5WVK; -.
DR PDBsum; 6EF3; -.
DR PDBsum; 6FVT; -.
DR PDBsum; 6FVU; -.
DR PDBsum; 6FVV; -.
DR PDBsum; 6FVW; -.
DR PDBsum; 6FVX; -.
DR PDBsum; 6FVY; -.
DR PDBsum; 6G7F; -.
DR PDBsum; 6G8M; -.
DR PDBsum; 6G8N; -.
DR PDBsum; 6GOP; -.
DR PDBsum; 6H39; -.
DR PDBsum; 6HTB; -.
DR PDBsum; 6HTC; -.
DR PDBsum; 6HTD; -.
DR PDBsum; 6HTP; -.
DR PDBsum; 6HTR; -.
DR PDBsum; 6HUB; -.
DR PDBsum; 6HUC; -.
DR PDBsum; 6HUQ; -.
DR PDBsum; 6HUU; -.
DR PDBsum; 6HUV; -.
DR PDBsum; 6HV3; -.
DR PDBsum; 6HV4; -.
DR PDBsum; 6HV5; -.
DR PDBsum; 6HV7; -.
DR PDBsum; 6HVA; -.
DR PDBsum; 6HVR; -.
DR PDBsum; 6HVS; -.
DR PDBsum; 6HVT; -.
DR PDBsum; 6HVU; -.
DR PDBsum; 6HVV; -.
DR PDBsum; 6HVW; -.
DR PDBsum; 6HVX; -.
DR PDBsum; 6HVY; -.
DR PDBsum; 6HW0; -.
DR PDBsum; 6HW3; -.
DR PDBsum; 6HW4; -.
DR PDBsum; 6HW5; -.
DR PDBsum; 6HW6; -.
DR PDBsum; 6HW7; -.
DR PDBsum; 6HW8; -.
DR PDBsum; 6HW9; -.
DR PDBsum; 6HWA; -.
DR PDBsum; 6HWB; -.
DR PDBsum; 6HWC; -.
DR PDBsum; 6HWD; -.
DR PDBsum; 6HWE; -.
DR PDBsum; 6HWF; -.
DR PDBsum; 6J2C; -.
DR PDBsum; 6J2N; -.
DR PDBsum; 6J2Q; -.
DR PDBsum; 6J2X; -.
DR PDBsum; 6J30; -.
DR PDBsum; 6ZOU; -.
DR PDBsum; 6ZP6; -.
DR PDBsum; 6ZP8; -.
DR PDBsum; 7LS5; -.
DR PDBsum; 7QO3; -.
DR PDBsum; 7QO5; -.
DR AlphaFoldDB; P38624; -.
DR SMR; P38624; -.
DR BioGRID; 33756; 123.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1527N; -.
DR IntAct; P38624; 23.
DR MINT; P38624; -.
DR STRING; 4932.YJL001W; -.
DR ChEMBL; CHEMBL4295578; -.
DR MEROPS; T01.010; -.
DR iPTMnet; P38624; -.
DR UCD-2DPAGE; P38624; -.
DR MaxQB; P38624; -.
DR PaxDb; P38624; -.
DR PRIDE; P38624; -.
DR EnsemblFungi; YJL001W_mRNA; YJL001W; YJL001W.
DR GeneID; 853456; -.
DR KEGG; sce:YJL001W; -.
DR SGD; S000003538; PRE3.
DR VEuPathDB; FungiDB:YJL001W; -.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000169029; -.
DR HOGENOM; CLU_035750_5_2_1; -.
DR InParanoid; P38624; -.
DR OMA; HKQAYAI; -.
DR BioCyc; YEAST:G3O-31481-MON; -.
DR BRENDA; 3.4.25.1; 984.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR EvolutionaryTrace; P38624; -.
DR PRO; PR:P38624; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P38624; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:SGD.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0004175; F:endopeptidase activity; IMP:SGD.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:SGD.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR037559; Proteasome_beta_Pre3.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF4; PTHR11599:SF4; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Nucleus; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..19
FT /note="Removed in mature form"
FT /id="PRO_0000026643"
FT CHAIN 20..215
FT /note="Proteasome subunit beta type-1"
FT /id="PRO_0000026644"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9087403"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:5FGI"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 68..89
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1JD2"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 167..184
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3SDK"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1RYP"
SQ SEQUENCE 215 AA; 23548 MW; BD1FCE649678D86B CRC64;
MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT DKLTRVHDKI
WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV FKELCYENKD NLTAGIIVAG
YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS TFIYGYCDKN FRENMSKEET VDFIKHSLSQ
AIKWDGSSGG VIRMVVLTAA GVERLIFYPD EYEQL
