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1CN1

CRYSTAL STRUCTURE OF DEMETALLIZED CONCANAVALIN A. THE METAL-BINDING REGION

Functional Information from GO Data
ChainGOidnamespacecontents
A0030246molecular_functioncarbohydrate binding
B0030246molecular_functioncarbohydrate binding
Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDT
ChainResidueDetails
AVAL5-THR11

site_idPS00308
Number of Residues10
DetailsLECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS
ChainResidueDetails
ALEU85-SER94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP208
BASP208

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P81461
ChainResidueDetails
AARG228
BARG228

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:34235541, ECO:0007744|PDB:6XT6
ChainResidueDetails
AGLY171
AALA173
ATRP182
AALA187
BGLY171
BALA173
BTRP182
BALA187

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:2792084, ECO:0000269|PubMed:34235541, ECO:0007744|PDB:6XT6
ChainResidueDetails
APHE175
AALA177
BPHE175
BALA177

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Cleavage
ChainResidueDetails
AASN237
AGLY163
BASN237
BGLY163

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AGLY152
BGLY152

222624

PDB entries from 2024-07-17

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