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3UBU

Crystal structure of agkisacucetin, a GpIb-binding snaclec (snake C-type lectin) that inhibits platelet

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 132
ChainResidue
ASER58
ASER87
ASER88
AGLY110
AARG112
AHOH142

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 127
ChainResidue
BTYR119
BHOH132
BLYS22
BSER64
BHIS118

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 128
ChainResidue
AGLN55
AARG112
BGLU12
BHIS14
BHIS45
BGLU49
BLYS123
BHOH140
BHOH184

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 129
ChainResidue
BASN75
BTRP92
BLYS102

Functional Information from PROSITE/UniProt
site_idPS00615
Number of Residues26
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CFvlekntgfrt..WLNLNCgseys.FVC
ChainResidueDetails
ACYS102-CYS127
BCYS98-CYS122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues117
DetailsDomain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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