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LEC1_PSOTE
ID   LEC1_PSOTE              Reviewed;         242 AA.
AC   O24313;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Basic agglutinin;
DE   AltName: Full=WBA I;
GN   Name=WBAI;
OS   Psophocarpus tetragonolobus (Winged bean) (Dolichos tetragonolobus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Psophocarpus.
OX   NCBI_TaxID=3891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8766718; DOI=10.1016/0014-5793(96)00613-8;
RA   Sharma V., Srinivas V.R., Surolia A.;
RT   "Cloning and sequencing of winged bean (Psophocarpus tetragonolobus) basic
RT   agglutinin (WBA I): presence of second glycosylation site and its
RT   implications in quaternary structure.";
RL   FEBS Lett. 389:289-292(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=9500920; DOI=10.1006/jmbi.1997.1568;
RA   Prabu M.M., Sankaranarayanan R., Puri K.D., Sharma V., Surolia A.,
RA   Vijayan M., Suguna K.;
RT   "Carbohydrate specificity and quaternary association in basic winged bean
RT   lectin: X-ray analysis of the lectin at 2.5-A resolution.";
RL   J. Mol. Biol. 276:787-796(1998).
CC   -!- FUNCTION: Lectin.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   EMBL; U60765; AAC49422.1; -; Genomic_DNA.
DR   PIR; S70467; S70467.
DR   PDB; 1WBF; X-ray; 2.30 A; A/B=1-242.
DR   PDB; 1WBL; X-ray; 2.50 A; A/B/C/D=2-242.
DR   PDB; 2D3S; X-ray; 2.35 A; A/B/C/D=1-242.
DR   PDB; 2DTW; X-ray; 2.40 A; A/B/C/D=2-242.
DR   PDB; 2DTY; X-ray; 2.65 A; A/B/C/D=2-242.
DR   PDB; 2DU0; X-ray; 2.70 A; A/B/C/D=2-242.
DR   PDB; 2DU1; X-ray; 2.60 A; A/B/C/D=2-242.
DR   PDB; 2E51; X-ray; 2.50 A; A/B/C/D=2-242.
DR   PDB; 2E53; X-ray; 2.40 A; A/B/C/D=2-242.
DR   PDB; 2E7Q; X-ray; 2.75 A; A/B/C/D=2-238.
DR   PDB; 2E7T; X-ray; 2.65 A; A/B/C/D=2-238.
DR   PDB; 2ZMK; X-ray; 2.50 A; A/B/C/D=2-242.
DR   PDB; 2ZML; X-ray; 2.65 A; A/B/C/D=2-242.
DR   PDB; 2ZMN; X-ray; 2.90 A; A/B/C/D=2-242.
DR   PDBsum; 1WBF; -.
DR   PDBsum; 1WBL; -.
DR   PDBsum; 2D3S; -.
DR   PDBsum; 2DTW; -.
DR   PDBsum; 2DTY; -.
DR   PDBsum; 2DU0; -.
DR   PDBsum; 2DU1; -.
DR   PDBsum; 2E51; -.
DR   PDBsum; 2E53; -.
DR   PDBsum; 2E7Q; -.
DR   PDBsum; 2E7T; -.
DR   PDBsum; 2ZMK; -.
DR   PDBsum; 2ZML; -.
DR   PDBsum; 2ZMN; -.
DR   AlphaFoldDB; O24313; -.
DR   SMR; O24313; -.
DR   UniLectin; O24313; -.
DR   EvolutionaryTrace; O24313; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016363; L-lectin.
DR   InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Lectin.
FT   CHAIN           1..242
FT                   /note="Basic agglutinin"
FT                   /id="PRO_0000105123"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          68..76
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:2ZMK"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          134..146
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   TURN            169..172
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   TURN            181..184
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          185..192
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   HELIX           195..198
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          201..211
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:1WBF"
FT   STRAND          226..235
FT                   /evidence="ECO:0007829|PDB:1WBF"
SQ   SEQUENCE   242 AA;  26615 MW;  8BD4368E26F72294 CRC64;
     MKTISFNFNQ FHQNEEQLKL QRDARISSNS VLELTKVVNG VPTWNSTGRA LYAKPVQVWD
     STTGNVASFE TRFSFSIRQP FPRPHPADGL VFFIAPPNTQ TGEGGGYFGI YNPLSPYPFV
     AVEFDTFRNT WDPQIPHIGI DVNSVISTKT VPFTLDNGGI ANVVIKYDAS TKILHVVLVF
     PSLGTIYTIA DIVDLKQVLP ESVNVGFSAA TGDPSGKQRN ATETHDILSW SFSASLPGTN
     EF
 
 
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