PYGM_RABIT
ID PYGM_RABIT Reviewed; 843 AA.
AC P00489;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Glycogen phosphorylase, muscle form {ECO:0000305|PubMed:3015680};
DE EC=2.4.1.1 {ECO:0000250|UniProtKB:P11217};
DE AltName: Full=Myophosphorylase;
GN Name=PYGM {ECO:0000250|UniProtKB:P11217};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT SER-2.
RX PubMed=3015680; DOI=10.1016/0014-5793(86)80829-8;
RA Nakano K., Hwang P.K., Fletterick R.J.;
RT "Complete cDNA sequence for rabbit muscle glycogen phosphorylase.";
RL FEBS Lett. 204:283-287(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-351.
RX PubMed=728424; DOI=10.1021/bi00619a012;
RA Koide A., Titani K., Ericsson L.H., Kumar S., Neurath H., Walsh K.A.;
RT "Sequence of the amino-terminal 349 residues of rabbit muscle glycogen
RT phosphorylase including the sites of covalent and allosteric control.";
RL Biochemistry 17:5657-5672(1978).
RN [3]
RP PROTEIN SEQUENCE OF 352-429 AND 443-605.
RX PubMed=728425; DOI=10.1021/bi00619a013;
RA Hermann J., Titani K., Ericsson L.H., Wade R.D., Neurath H., Walsh K.A.;
RT "Amino acid sequence of two cyanogen bromide fragments of glycogen
RT phosphorylase.";
RL Biochemistry 17:5672-5679(1978).
RN [4]
RP PROTEIN SEQUENCE OF 352-843.
RX PubMed=728426; DOI=10.1021/bi00619a014;
RA Titani K., Koide A., Ericsson L.H., Kumar S., Hermann J., Wade R.D.,
RA Walsh K.A., Neurath H., Fischer E.H.;
RT "Sequence of the carboxyl-terminal 492 residues of rabbit muscle glycogen
RT phosphorylase including the pyridoxal 5'-phosphate binding site.";
RL Biochemistry 17:5680-5693(1978).
RN [5]
RP PROTEIN SEQUENCE OF 71-81.
RX PubMed=670209; DOI=10.1016/s0021-9258(17)30395-2;
RA Lee Y.M., Benisek W.F.;
RT "Inactivation of phosphorylase b by potassium ferrate. Identification of a
RT tyrosine residue involved in the binding of adenosine 5'-monophosphate.";
RL J. Biol. Chem. 253:5460-5463(1978).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 575-843.
RX PubMed=3840433; DOI=10.1111/j.1432-1033.1985.tb09193.x;
RA Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J.,
RA Crerar M.M.;
RT "Comparative sequence analysis of rat, rabbit, and human muscle glycogen
RT phosphorylase cDNAs.";
RL Eur. J. Biochem. 152:267-274(1985).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A.
RX PubMed=728427;
RA Sprang S.R., Fletterick R.J.;
RT "Crystallographic analysis of phosphorylase alpha at 2.5-A resolution, a
RT comment on the chemical sequence.";
RL Biochemistry 17:5693-5694(1978).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF PHOSPHORYLASE A.
RX PubMed=2756432; DOI=10.1126/science.2756432;
RA Goldsmith E.J., Sprang S.R., Hamlin R., Xuong N.-H., Fletterick R.J.;
RT "Domain separation in the activation of glycogen phosphorylase a.";
RL Science 245:528-532(1989).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A WITH AMP.
RX PubMed=3616621; DOI=10.1126/science.3616621;
RA Sprang S.R., Goldsmith E.J., Fletterick R.J.;
RT "Structure of the nucleotide activation switch in glycogen phosphorylase
RT a.";
RL Science 237:1012-1019(1987).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PHOSPHORYLASE B.
RX PubMed=728428;
RA Jenkins J.A., Johnson L.N., Wilson K.S.;
RT "Assignment of the amino acid sequence to the crystal structure of glycogen
RT phosphorylase b.";
RL Biochemistry 17:5694-5695(1978).
RN [11] {ECO:0007744|PDB:2PRI}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF PHOSPHORYLASE B.
RX PubMed=7500360; DOI=10.1006/jmbi.1995.0665;
RA Oikonomakos N.G., Zographos S.E., Johnson L.N., Papageorgiou A.C.,
RA Acharya K.R.;
RT "The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b:
RT kinetic and crystallographic studies.";
RL J. Mol. Biol. 254:900-917(1995).
RN [12] {ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PHOSPHORYLASE B.
RX PubMed=8976550; DOI=10.1002/pro.5560051204;
RA Oikonomakos N.G., Zographos S.E., Tsitsanou K.E., Johnson L.N.,
RA Acharya K.R.;
RT "Activator anion binding site in pyridoxal phosphorylase b: the binding of
RT phosphite, phosphate, and fluorophosphate in the crystal.";
RL Protein Sci. 5:2416-2428(1996).
RN [13] {ECO:0007744|PDB:1A8I, ECO:0007744|PDB:2GPN}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF PHOSPHORYLASE B.
RX PubMed=9568898; DOI=10.1002/pro.5560070409;
RA Gregoriou M., Noble M.E.M., Watson K.A., Garman E.F., Krulle T.M.,
RA de la Fuente C., Fleet G.W., Oikonomakos N.G., Johnson L.N.;
RT "The structure of a glycogen phosphorylase glucopyranose spirohydantoin
RT complex at 1.8-A resolution and 100 K: the role of the water structure and
RT its contribution to binding.";
RL Protein Sci. 7:915-927(1998).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000250|UniProtKB:P11217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000250|UniProtKB:P11217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000250|UniProtKB:P11217};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550,
CC ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD,
CC ECO:0007744|PDB:2SKE};
CC -!- ACTIVITY REGULATION: Allosterically regulated through the non-covalent
CC binding of metabolites, being activated by AMP and inhibited by ATP,
CC ADP, and glucose-6-phosphate. The activity is also controlled by post-
CC translational modifications including phosphorylation.
CC {ECO:0000250|UniProtKB:P11217}.
CC -!- SUBUNIT: Homodimer. Homotetramer; to form the enzymatically active
CC phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
CC (unphosphorylated) to phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; D00040; BAA00027.1; -; mRNA.
DR EMBL; X04265; CAA27816.1; -; mRNA.
DR EMBL; X03030; CAA26833.1; -; mRNA.
DR PIR; A24302; PHRBG.
DR RefSeq; NP_001075653.1; NM_001082184.1.
DR PDB; 1A8I; X-ray; 1.78 A; A=2-843.
DR PDB; 1ABB; X-ray; 2.80 A; A/B/C/D=11-838.
DR PDB; 1AXR; X-ray; 2.30 A; A=2-843.
DR PDB; 1B4D; X-ray; 2.00 A; A=2-843.
DR PDB; 1BX3; X-ray; 2.30 A; A=2-843.
DR PDB; 1C50; X-ray; 2.30 A; A=14-843.
DR PDB; 1C8K; X-ray; 1.76 A; A=2-843.
DR PDB; 1C8L; X-ray; 2.30 A; A=2-843.
DR PDB; 1E1Y; X-ray; 2.23 A; A=2-843.
DR PDB; 1FS4; X-ray; 2.38 A; A=2-843.
DR PDB; 1FTQ; X-ray; 2.35 A; A=2-843.
DR PDB; 1FTW; X-ray; 2.36 A; A=2-843.
DR PDB; 1FTY; X-ray; 2.38 A; A=2-843.
DR PDB; 1FU4; X-ray; 2.36 A; A=2-843.
DR PDB; 1FU7; X-ray; 2.36 A; A=2-843.
DR PDB; 1FU8; X-ray; 2.35 A; A=2-843.
DR PDB; 1GFZ; X-ray; 2.30 A; A=2-843.
DR PDB; 1GG8; X-ray; 2.31 A; A=2-843.
DR PDB; 1GGN; X-ray; 2.36 A; A=2-843.
DR PDB; 1GPA; X-ray; 2.90 A; A/B/C/D=2-843.
DR PDB; 1GPB; X-ray; 1.90 A; A=2-843.
DR PDB; 1GPY; X-ray; 2.40 A; A=2-843.
DR PDB; 1H5U; X-ray; 1.76 A; A=2-843.
DR PDB; 1HLF; X-ray; 2.26 A; A=2-843.
DR PDB; 1K06; X-ray; 1.80 A; A=2-843.
DR PDB; 1K08; X-ray; 2.26 A; A=2-843.
DR PDB; 1KTI; X-ray; 1.97 A; A=2-843.
DR PDB; 1LWN; X-ray; 2.00 A; A=2-843.
DR PDB; 1LWO; X-ray; 2.00 A; A=2-843.
DR PDB; 1NOI; X-ray; 2.50 A; A/B/C/D=2-843.
DR PDB; 1NOJ; X-ray; 2.40 A; A=2-843.
DR PDB; 1NOK; X-ray; 2.40 A; A=2-843.
DR PDB; 1P29; X-ray; 2.20 A; A=2-843.
DR PDB; 1P2B; X-ray; 2.20 A; A=2-843.
DR PDB; 1P2D; X-ray; 1.94 A; A=2-843.
DR PDB; 1P2G; X-ray; 2.30 A; A=2-843.
DR PDB; 1P4G; X-ray; 2.10 A; A=2-843.
DR PDB; 1P4H; X-ray; 2.06 A; A=2-843.
DR PDB; 1P4J; X-ray; 2.00 A; A=2-843.
DR PDB; 1PYG; X-ray; 2.87 A; A/B/C/D=2-843.
DR PDB; 1UZU; X-ray; 2.30 A; A=2-843.
DR PDB; 1WUT; X-ray; 2.26 A; A=2-843.
DR PDB; 1WUY; X-ray; 2.26 A; A=2-843.
DR PDB; 1WV0; X-ray; 2.26 A; A=2-843.
DR PDB; 1WV1; X-ray; 2.26 A; A=2-843.
DR PDB; 1WW2; X-ray; 1.90 A; A=2-843.
DR PDB; 1WW3; X-ray; 1.80 A; A=2-843.
DR PDB; 1XC7; X-ray; 1.83 A; A=2-843.
DR PDB; 1XKX; X-ray; 1.93 A; A=2-843.
DR PDB; 1XL0; X-ray; 1.92 A; A=2-843.
DR PDB; 1XL1; X-ray; 2.10 A; A=2-843.
DR PDB; 1Z62; X-ray; 1.90 A; A=2-843.
DR PDB; 1Z6P; X-ray; 2.40 A; A=2-843.
DR PDB; 1Z6Q; X-ray; 2.03 A; A=2-843.
DR PDB; 2AMV; X-ray; 2.30 A; A=2-843.
DR PDB; 2F3P; X-ray; 1.94 A; A=2-843.
DR PDB; 2F3Q; X-ray; 1.96 A; A=2-843.
DR PDB; 2F3S; X-ray; 1.96 A; A=2-843.
DR PDB; 2F3U; X-ray; 1.93 A; A=2-843.
DR PDB; 2FET; X-ray; 2.03 A; A=2-843.
DR PDB; 2FF5; X-ray; 2.03 A; A=2-843.
DR PDB; 2FFR; X-ray; 2.03 A; A=13-837.
DR PDB; 2G9Q; X-ray; 2.50 A; A=2-843.
DR PDB; 2G9R; X-ray; 2.07 A; A=2-843.
DR PDB; 2G9U; X-ray; 2.15 A; A=2-843.
DR PDB; 2G9V; X-ray; 2.15 A; A=2-843.
DR PDB; 2GJ4; X-ray; 1.60 A; A=13-836.
DR PDB; 2GM9; X-ray; 2.30 A; A=13-837.
DR PDB; 2GPA; X-ray; 2.00 A; A=2-843.
DR PDB; 2GPB; X-ray; 2.30 A; A=2-843.
DR PDB; 2GPN; X-ray; 1.99 A; A=2-843.
DR PDB; 2IEG; X-ray; 1.90 A; A/B=2-843.
DR PDB; 2IEI; X-ray; 1.91 A; A/B=2-843.
DR PDB; 2OFF; X-ray; 2.20 A; A=2-843.
DR PDB; 2PRI; X-ray; 2.30 A; A=2-843.
DR PDB; 2PRJ; X-ray; 2.30 A; A=2-843.
DR PDB; 2PYD; X-ray; 1.93 A; A=1-843.
DR PDB; 2PYI; X-ray; 1.88 A; A=1-843.
DR PDB; 2QLM; X-ray; 2.10 A; A=2-843.
DR PDB; 2QLN; X-ray; 2.15 A; A=2-843.
DR PDB; 2QN1; X-ray; 2.40 A; A=2-843.
DR PDB; 2QN2; X-ray; 2.70 A; A=2-843.
DR PDB; 2QN3; X-ray; 1.96 A; A=2-843.
DR PDB; 2QN7; X-ray; 1.83 A; A=2-843.
DR PDB; 2QN8; X-ray; 1.90 A; A=2-843.
DR PDB; 2QN9; X-ray; 2.00 A; A=2-843.
DR PDB; 2QNB; X-ray; 1.80 A; A=2-843.
DR PDB; 2QRG; X-ray; 1.85 A; A=2-843.
DR PDB; 2QRH; X-ray; 1.83 A; A=2-843.
DR PDB; 2QRM; X-ray; 1.90 A; A=2-843.
DR PDB; 2QRP; X-ray; 1.86 A; A=2-843.
DR PDB; 2QRQ; X-ray; 1.80 A; A=2-843.
DR PDB; 2SKC; X-ray; 2.40 A; A=2-843.
DR PDB; 2SKD; X-ray; 2.40 A; A=2-843.
DR PDB; 2SKE; X-ray; 2.46 A; A=2-843.
DR PDB; 3AMV; X-ray; 2.10 A; A=2-843.
DR PDB; 3BCR; X-ray; 2.14 A; A=2-843.
DR PDB; 3BCS; X-ray; 2.00 A; A=2-843.
DR PDB; 3BCU; X-ray; 2.03 A; A=2-843.
DR PDB; 3BD6; X-ray; 2.00 A; A=2-843.
DR PDB; 3BD7; X-ray; 1.90 A; A=2-843.
DR PDB; 3BD8; X-ray; 2.10 A; A=2-843.
DR PDB; 3BDA; X-ray; 2.00 A; A=2-843.
DR PDB; 3CUT; X-ray; 2.30 A; A=2-843.
DR PDB; 3CUU; X-ray; 2.30 A; A=2-843.
DR PDB; 3CUV; X-ray; 1.93 A; A=2-843.
DR PDB; 3CUW; X-ray; 2.00 A; A=2-843.
DR PDB; 3E3L; X-ray; 2.59 A; A/B/C/D=2-843.
DR PDB; 3E3N; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-843.
DR PDB; 3E3O; X-ray; 2.60 A; A/B/C/D=2-843.
DR PDB; 3EBO; X-ray; 1.90 A; A=2-843.
DR PDB; 3EBP; X-ray; 2.00 A; A=2-843.
DR PDB; 3G2H; X-ray; 2.03 A; A=2-843.
DR PDB; 3G2I; X-ray; 2.00 A; A=2-843.
DR PDB; 3G2J; X-ray; 2.14 A; A=2-843.
DR PDB; 3G2K; X-ray; 2.00 A; A=2-843.
DR PDB; 3G2L; X-ray; 2.30 A; A=2-843.
DR PDB; 3G2N; X-ray; 2.10 A; A=2-843.
DR PDB; 3GPB; X-ray; 2.30 A; A=2-843.
DR PDB; 3L79; X-ray; 1.86 A; A=1-843.
DR PDB; 3L7A; X-ray; 1.90 A; A=1-843.
DR PDB; 3L7B; X-ray; 2.00 A; A=1-843.
DR PDB; 3L7C; X-ray; 1.93 A; A=1-843.
DR PDB; 3L7D; X-ray; 2.00 A; A=1-843.
DR PDB; 3MQF; X-ray; 1.95 A; A=2-843.
DR PDB; 3MRT; X-ray; 1.98 A; A=2-843.
DR PDB; 3MRV; X-ray; 1.94 A; A=2-843.
DR PDB; 3MRX; X-ray; 1.95 A; A=2-843.
DR PDB; 3MS2; X-ray; 2.10 A; A=2-843.
DR PDB; 3MS4; X-ray; 2.07 A; A=2-843.
DR PDB; 3MS7; X-ray; 1.95 A; A=2-843.
DR PDB; 3MSC; X-ray; 1.95 A; A=2-843.
DR PDB; 3MT7; X-ray; 2.00 A; A=2-843.
DR PDB; 3MT8; X-ray; 2.00 A; A=2-843.
DR PDB; 3MT9; X-ray; 2.05 A; A=2-843.
DR PDB; 3MTA; X-ray; 2.23 A; A=2-843.
DR PDB; 3MTB; X-ray; 1.95 A; A=2-843.
DR PDB; 3MTD; X-ray; 2.10 A; A=2-843.
DR PDB; 3NC4; X-ray; 2.07 A; A=3-843.
DR PDB; 3NP7; X-ray; 2.05 A; A=2-843.
DR PDB; 3NP9; X-ray; 2.00 A; A=2-843.
DR PDB; 3NPA; X-ray; 1.97 A; A=2-843.
DR PDB; 3S0J; X-ray; 2.00 A; A=2-843.
DR PDB; 3SYM; X-ray; 2.40 A; A=2-843.
DR PDB; 3SYR; X-ray; 2.40 A; A=2-843.
DR PDB; 3T3D; X-ray; 2.50 A; A=2-843.
DR PDB; 3T3E; X-ray; 2.15 A; A=2-843.
DR PDB; 3T3G; X-ray; 2.40 A; A=2-843.
DR PDB; 3T3H; X-ray; 2.60 A; A=2-843.
DR PDB; 3T3I; X-ray; 2.65 A; A=2-843.
DR PDB; 3ZCP; X-ray; 1.83 A; A=1-843.
DR PDB; 3ZCQ; X-ray; 2.15 A; A=1-843.
DR PDB; 3ZCR; X-ray; 2.07 A; A=1-843.
DR PDB; 3ZCS; X-ray; 2.03 A; A=1-843.
DR PDB; 3ZCT; X-ray; 2.00 A; A=1-843.
DR PDB; 3ZCU; X-ray; 2.05 A; A=1-843.
DR PDB; 3ZCV; X-ray; 1.83 A; A=1-843.
DR PDB; 4CTM; X-ray; 1.95 A; A=1-843.
DR PDB; 4CTN; X-ray; 2.10 A; A=1-843.
DR PDB; 4CTO; X-ray; 1.90 A; A=1-843.
DR PDB; 4EJ2; X-ray; 2.65 A; A=13-837.
DR PDB; 4EKE; X-ray; 2.60 A; A=13-837.
DR PDB; 4EKY; X-ray; 2.45 A; A=13-837.
DR PDB; 4EL0; X-ray; 2.40 A; A=13-837.
DR PDB; 4EL5; X-ray; 2.00 A; A=13-837.
DR PDB; 4GPB; X-ray; 2.30 A; A=2-843.
DR PDB; 4MHO; X-ray; 2.00 A; A=13-837.
DR PDB; 4MHS; X-ray; 2.00 A; A=13-837.
DR PDB; 4MI3; X-ray; 2.15 A; A=13-837.
DR PDB; 4MI6; X-ray; 1.90 A; A=13-837.
DR PDB; 4MI9; X-ray; 1.85 A; A=13-837.
DR PDB; 4MIC; X-ray; 2.45 A; A=13-837.
DR PDB; 4MRA; X-ray; 2.34 A; A=13-837.
DR PDB; 4YI3; X-ray; 1.80 A; A=1-843.
DR PDB; 4YI5; X-ray; 1.80 A; A=1-843.
DR PDB; 4YUA; X-ray; 2.00 A; A=13-837.
DR PDB; 4Z5X; X-ray; 2.10 A; A=1-843.
DR PDB; 5GPB; X-ray; 2.30 A; A=2-843.
DR PDB; 5JTT; X-ray; 1.85 A; A=1-843.
DR PDB; 5JTU; X-ray; 1.85 A; A=1-843.
DR PDB; 5LRC; X-ray; 2.00 A; A=2-843.
DR PDB; 5LRD; X-ray; 1.80 A; A=1-843.
DR PDB; 5LRE; X-ray; 1.80 A; A=2-843.
DR PDB; 5LRF; X-ray; 1.75 A; A=2-843.
DR PDB; 5MCB; X-ray; 1.95 A; A=13-837.
DR PDB; 5MEM; X-ray; 1.78 A; A=1-843.
DR PDB; 5O50; X-ray; 1.90 A; A=2-843.
DR PDB; 5O52; X-ray; 1.90 A; A=1-843.
DR PDB; 5O54; X-ray; 2.45 A; A=1-843.
DR PDB; 5O56; X-ray; 2.45 A; A=1-843.
DR PDB; 5OWY; X-ray; 1.90 A; A=1-843.
DR PDB; 5OWZ; X-ray; 1.85 A; A=1-843.
DR PDB; 5OX0; X-ray; 1.90 A; A=1-843.
DR PDB; 5OX1; X-ray; 1.85 A; A=1-843.
DR PDB; 5OX3; X-ray; 1.90 A; A=1-843.
DR PDB; 5OX4; X-ray; 1.80 A; A=1-843.
DR PDB; 6F3J; X-ray; 2.20 A; A=1-843.
DR PDB; 6F3L; X-ray; 1.90 A; A=1-843.
DR PDB; 6F3R; X-ray; 1.90 A; A=1-843.
DR PDB; 6F3S; X-ray; 1.90 A; A=1-843.
DR PDB; 6F3U; X-ray; 2.20 A; A=1-843.
DR PDB; 6GPB; X-ray; 2.86 A; A=2-843.
DR PDB; 6QA6; X-ray; 2.40 A; A=1-843.
DR PDB; 6QA7; X-ray; 2.36 A; A=1-843.
DR PDB; 6QA8; X-ray; 2.35 A; A=1-843.
DR PDB; 6R0H; X-ray; 2.50 A; A=1-843.
DR PDB; 6R0I; X-ray; 2.40 A; A=1-843.
DR PDB; 6S4H; X-ray; 2.45 A; A=1-843.
DR PDB; 6S4K; X-ray; 2.43 A; A=1-843.
DR PDB; 6S4O; X-ray; 2.35 A; A=1-843.
DR PDB; 6S4P; X-ray; 2.37 A; A=1-843.
DR PDB; 6S4R; X-ray; 2.30 A; A=1-843.
DR PDB; 6S51; X-ray; 2.37 A; A=1-843.
DR PDB; 6S52; X-ray; 2.37 A; A=1-843.
DR PDB; 6Y55; X-ray; 2.38 A; A=1-843.
DR PDB; 6Y5C; X-ray; 2.40 A; A=2-843.
DR PDB; 6Y5O; X-ray; 2.33 A; A=2-843.
DR PDB; 6YVE; X-ray; 2.10 A; AAA=1-843.
DR PDB; 7GPB; X-ray; 2.90 A; A/B/C/D=2-843.
DR PDB; 7ONF; X-ray; 1.60 A; A=13-837.
DR PDB; 7P7D; X-ray; 1.45 A; A=8-837.
DR PDB; 7Q5I; X-ray; 1.80 A; AAA=1-843.
DR PDB; 8GPB; X-ray; 2.20 A; A=2-843.
DR PDB; 9GPB; X-ray; 2.90 A; A/B/C/D=2-843.
DR PDBsum; 1A8I; -.
DR PDBsum; 1ABB; -.
DR PDBsum; 1AXR; -.
DR PDBsum; 1B4D; -.
DR PDBsum; 1BX3; -.
DR PDBsum; 1C50; -.
DR PDBsum; 1C8K; -.
DR PDBsum; 1C8L; -.
DR PDBsum; 1E1Y; -.
DR PDBsum; 1FS4; -.
DR PDBsum; 1FTQ; -.
DR PDBsum; 1FTW; -.
DR PDBsum; 1FTY; -.
DR PDBsum; 1FU4; -.
DR PDBsum; 1FU7; -.
DR PDBsum; 1FU8; -.
DR PDBsum; 1GFZ; -.
DR PDBsum; 1GG8; -.
DR PDBsum; 1GGN; -.
DR PDBsum; 1GPA; -.
DR PDBsum; 1GPB; -.
DR PDBsum; 1GPY; -.
DR PDBsum; 1H5U; -.
DR PDBsum; 1HLF; -.
DR PDBsum; 1K06; -.
DR PDBsum; 1K08; -.
DR PDBsum; 1KTI; -.
DR PDBsum; 1LWN; -.
DR PDBsum; 1LWO; -.
DR PDBsum; 1NOI; -.
DR PDBsum; 1NOJ; -.
DR PDBsum; 1NOK; -.
DR PDBsum; 1P29; -.
DR PDBsum; 1P2B; -.
DR PDBsum; 1P2D; -.
DR PDBsum; 1P2G; -.
DR PDBsum; 1P4G; -.
DR PDBsum; 1P4H; -.
DR PDBsum; 1P4J; -.
DR PDBsum; 1PYG; -.
DR PDBsum; 1UZU; -.
DR PDBsum; 1WUT; -.
DR PDBsum; 1WUY; -.
DR PDBsum; 1WV0; -.
DR PDBsum; 1WV1; -.
DR PDBsum; 1WW2; -.
DR PDBsum; 1WW3; -.
DR PDBsum; 1XC7; -.
DR PDBsum; 1XKX; -.
DR PDBsum; 1XL0; -.
DR PDBsum; 1XL1; -.
DR PDBsum; 1Z62; -.
DR PDBsum; 1Z6P; -.
DR PDBsum; 1Z6Q; -.
DR PDBsum; 2AMV; -.
DR PDBsum; 2F3P; -.
DR PDBsum; 2F3Q; -.
DR PDBsum; 2F3S; -.
DR PDBsum; 2F3U; -.
DR PDBsum; 2FET; -.
DR PDBsum; 2FF5; -.
DR PDBsum; 2FFR; -.
DR PDBsum; 2G9Q; -.
DR PDBsum; 2G9R; -.
DR PDBsum; 2G9U; -.
DR PDBsum; 2G9V; -.
DR PDBsum; 2GJ4; -.
DR PDBsum; 2GM9; -.
DR PDBsum; 2GPA; -.
DR PDBsum; 2GPB; -.
DR PDBsum; 2GPN; -.
DR PDBsum; 2IEG; -.
DR PDBsum; 2IEI; -.
DR PDBsum; 2OFF; -.
DR PDBsum; 2PRI; -.
DR PDBsum; 2PRJ; -.
DR PDBsum; 2PYD; -.
DR PDBsum; 2PYI; -.
DR PDBsum; 2QLM; -.
DR PDBsum; 2QLN; -.
DR PDBsum; 2QN1; -.
DR PDBsum; 2QN2; -.
DR PDBsum; 2QN3; -.
DR PDBsum; 2QN7; -.
DR PDBsum; 2QN8; -.
DR PDBsum; 2QN9; -.
DR PDBsum; 2QNB; -.
DR PDBsum; 2QRG; -.
DR PDBsum; 2QRH; -.
DR PDBsum; 2QRM; -.
DR PDBsum; 2QRP; -.
DR PDBsum; 2QRQ; -.
DR PDBsum; 2SKC; -.
DR PDBsum; 2SKD; -.
DR PDBsum; 2SKE; -.
DR PDBsum; 3AMV; -.
DR PDBsum; 3BCR; -.
DR PDBsum; 3BCS; -.
DR PDBsum; 3BCU; -.
DR PDBsum; 3BD6; -.
DR PDBsum; 3BD7; -.
DR PDBsum; 3BD8; -.
DR PDBsum; 3BDA; -.
DR PDBsum; 3CUT; -.
DR PDBsum; 3CUU; -.
DR PDBsum; 3CUV; -.
DR PDBsum; 3CUW; -.
DR PDBsum; 3E3L; -.
DR PDBsum; 3E3N; -.
DR PDBsum; 3E3O; -.
DR PDBsum; 3EBO; -.
DR PDBsum; 3EBP; -.
DR PDBsum; 3G2H; -.
DR PDBsum; 3G2I; -.
DR PDBsum; 3G2J; -.
DR PDBsum; 3G2K; -.
DR PDBsum; 3G2L; -.
DR PDBsum; 3G2N; -.
DR PDBsum; 3GPB; -.
DR PDBsum; 3L79; -.
DR PDBsum; 3L7A; -.
DR PDBsum; 3L7B; -.
DR PDBsum; 3L7C; -.
DR PDBsum; 3L7D; -.
DR PDBsum; 3MQF; -.
DR PDBsum; 3MRT; -.
DR PDBsum; 3MRV; -.
DR PDBsum; 3MRX; -.
DR PDBsum; 3MS2; -.
DR PDBsum; 3MS4; -.
DR PDBsum; 3MS7; -.
DR PDBsum; 3MSC; -.
DR PDBsum; 3MT7; -.
DR PDBsum; 3MT8; -.
DR PDBsum; 3MT9; -.
DR PDBsum; 3MTA; -.
DR PDBsum; 3MTB; -.
DR PDBsum; 3MTD; -.
DR PDBsum; 3NC4; -.
DR PDBsum; 3NP7; -.
DR PDBsum; 3NP9; -.
DR PDBsum; 3NPA; -.
DR PDBsum; 3S0J; -.
DR PDBsum; 3SYM; -.
DR PDBsum; 3SYR; -.
DR PDBsum; 3T3D; -.
DR PDBsum; 3T3E; -.
DR PDBsum; 3T3G; -.
DR PDBsum; 3T3H; -.
DR PDBsum; 3T3I; -.
DR PDBsum; 3ZCP; -.
DR PDBsum; 3ZCQ; -.
DR PDBsum; 3ZCR; -.
DR PDBsum; 3ZCS; -.
DR PDBsum; 3ZCT; -.
DR PDBsum; 3ZCU; -.
DR PDBsum; 3ZCV; -.
DR PDBsum; 4CTM; -.
DR PDBsum; 4CTN; -.
DR PDBsum; 4CTO; -.
DR PDBsum; 4EJ2; -.
DR PDBsum; 4EKE; -.
DR PDBsum; 4EKY; -.
DR PDBsum; 4EL0; -.
DR PDBsum; 4EL5; -.
DR PDBsum; 4GPB; -.
DR PDBsum; 4MHO; -.
DR PDBsum; 4MHS; -.
DR PDBsum; 4MI3; -.
DR PDBsum; 4MI6; -.
DR PDBsum; 4MI9; -.
DR PDBsum; 4MIC; -.
DR PDBsum; 4MRA; -.
DR PDBsum; 4YI3; -.
DR PDBsum; 4YI5; -.
DR PDBsum; 4YUA; -.
DR PDBsum; 4Z5X; -.
DR PDBsum; 5GPB; -.
DR PDBsum; 5JTT; -.
DR PDBsum; 5JTU; -.
DR PDBsum; 5LRC; -.
DR PDBsum; 5LRD; -.
DR PDBsum; 5LRE; -.
DR PDBsum; 5LRF; -.
DR PDBsum; 5MCB; -.
DR PDBsum; 5MEM; -.
DR PDBsum; 5O50; -.
DR PDBsum; 5O52; -.
DR PDBsum; 5O54; -.
DR PDBsum; 5O56; -.
DR PDBsum; 5OWY; -.
DR PDBsum; 5OWZ; -.
DR PDBsum; 5OX0; -.
DR PDBsum; 5OX1; -.
DR PDBsum; 5OX3; -.
DR PDBsum; 5OX4; -.
DR PDBsum; 6F3J; -.
DR PDBsum; 6F3L; -.
DR PDBsum; 6F3R; -.
DR PDBsum; 6F3S; -.
DR PDBsum; 6F3U; -.
DR PDBsum; 6GPB; -.
DR PDBsum; 6QA6; -.
DR PDBsum; 6QA7; -.
DR PDBsum; 6QA8; -.
DR PDBsum; 6R0H; -.
DR PDBsum; 6R0I; -.
DR PDBsum; 6S4H; -.
DR PDBsum; 6S4K; -.
DR PDBsum; 6S4O; -.
DR PDBsum; 6S4P; -.
DR PDBsum; 6S4R; -.
DR PDBsum; 6S51; -.
DR PDBsum; 6S52; -.
DR PDBsum; 6Y55; -.
DR PDBsum; 6Y5C; -.
DR PDBsum; 6Y5O; -.
DR PDBsum; 6YVE; -.
DR PDBsum; 7GPB; -.
DR PDBsum; 7ONF; -.
DR PDBsum; 7P7D; -.
DR PDBsum; 7Q5I; -.
DR PDBsum; 8GPB; -.
DR PDBsum; 9GPB; -.
DR AlphaFoldDB; P00489; -.
DR PCDDB; P00489; -.
DR SMR; P00489; -.
DR DIP; DIP-38240N; -.
DR ELM; P00489; -.
DR IntAct; P00489; 5.
DR MINT; P00489; -.
DR STRING; 9986.ENSOCUP00000001880; -.
DR BindingDB; P00489; -.
DR ChEMBL; CHEMBL4696; -.
DR DrugCentral; P00489; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; P00489; -.
DR PRIDE; P00489; -.
DR GeneID; 100008972; -.
DR KEGG; ocu:100008972; -.
DR CTD; 5837; -.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; P00489; -.
DR OrthoDB; 240595at2759; -.
DR BRENDA; 2.4.1.1; 1749.
DR SABIO-RK; P00489; -.
DR EvolutionaryTrace; P00489; -.
DR PRO; PR:P00489; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR GO; GO:0008184; F:glycogen phosphorylase activity; ISS:UniProtKB.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; ISS:UniProtKB.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW Direct protein sequencing; Glycogen metabolism; Glycosyltransferase;
KW Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:728424"
FT CHAIN 2..843
FT /note="Glycogen phosphorylase, muscle form"
FT /id="PRO_0000188532"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT BINDING 76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:3616621"
FT BINDING 310..319
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT SITE 109
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000303|PubMed:728424"
FT SITE 143
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000303|PubMed:728424"
FT SITE 156
FT /note="Can be labeled by an AMP analog; may be involved in
FT allosteric regulation"
FT /evidence="ECO:0000303|PubMed:728424"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3015680"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase A"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT MOD_RES 204
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB3"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB3"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:7500360,
FT ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI,
FT ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD,
FT ECO:0007744|PDB:2SKE"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT CONFLICT 31..33
FT /note="NFN -> DFD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..58
FT /note="LAH -> HAL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="T -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 578..579
FT /note="LL -> FF (in Ref. 6; CAA26833)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="A -> P (in Ref. 1; BAA00027/CAA27816)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="G -> C (in Ref. 6; CAA26833)"
FT /evidence="ECO:0000305"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 22..38
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 211..232
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:5LRF"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1GPA"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1C8K"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2QRQ"
FT HELIX 291..313
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 315..319
FT /evidence="ECO:0007829|PDB:1C8K"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1GPB"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:3E3L"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 498..508
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 516..525
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 529..554
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 577..593
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 615..631
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 641..646
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:2QNB"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:1Z6P"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:3E3L"
FT TURN 683..686
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 697..704
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 716..725
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 729..735
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 737..748
FT /evidence="ECO:0007829|PDB:7P7D"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:7P7D"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:1C8K"
FT TURN 756..759
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 760..768
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 774..792
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 795..806
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:7P7D"
FT HELIX 814..824
FT /evidence="ECO:0007829|PDB:7P7D"
SQ SEQUENCE 843 AA; 97289 MW; 9884F06FDD3AE9D3 CRC64;
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRVLVDLERL
DWDKAWEVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEIIAERIGE EYISDLDQLR KLLSYVDDEA FIRDVAKVKQ
ENKLKFAAYL EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFVV
PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE
YVKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE
KIP
