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3I03

Crystal structure of bothropstoxin-I chemically modified by p-bromophenacyl bromide (BPB) - monomeric form at a high resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006644biological_processphospholipid metabolic process
A0008201molecular_functionheparin binding
A0016042biological_processlipid catabolic process
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0042742biological_processdefense response to bacterium
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PBP A 201
ChainResidue
ATYR21
AHOH473
AHOH479
AHOH618
AGLY22
ACYS28
AGLY29
ACYS44
AHIS47
AVAL92
AHOH325
AHOH461

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA A 211
ChainResidue
ALEU2
AALA18

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYvHKcC
ChainResidueDetails
ACYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC
ChainResidueDetails
ALEU85-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
ALYS105

221051

PDB entries from 2024-06-12

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