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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2QOG

Crotoxin B, the basic PLA2 from Crotalus durissus terrificus.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
A0099106molecular_functionion channel regulator activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0042130biological_processnegative regulation of T cell proliferation
B0044398biological_processvenom-mediated edema
B0044478biological_processvenom-mediated platelet aggregation
B0044521biological_processvenom-mediated muscle damage in another organism
B0044522biological_processvenom-mediated myocyte killing in another organism
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonate secretion
B0090729molecular_functiontoxin activity
B0099106molecular_functionion channel regulator activity
C0004623molecular_functionphospholipase A2 activity
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006629biological_processlipid metabolic process
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0016787molecular_functionhydrolase activity
C0042130biological_processnegative regulation of T cell proliferation
C0044398biological_processvenom-mediated edema
C0044478biological_processvenom-mediated platelet aggregation
C0044521biological_processvenom-mediated muscle damage in another organism
C0044522biological_processvenom-mediated myocyte killing in another organism
C0046872molecular_functionmetal ion binding
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonate secretion
C0090729molecular_functiontoxin activity
C0099106molecular_functionion channel regulator activity
D0004623molecular_functionphospholipase A2 activity
D0005509molecular_functioncalcium ion binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
D0006629biological_processlipid metabolic process
D0006644biological_processphospholipid metabolic process
D0016042biological_processlipid catabolic process
D0016787molecular_functionhydrolase activity
D0035821biological_processmodulation of process of another organism
D0042130biological_processnegative regulation of T cell proliferation
D0046872molecular_functionmetal ion binding
D0047498molecular_functioncalcium-dependent phospholipase A2 activity
D0050482biological_processarachidonate secretion
D0090729molecular_functiontoxin activity
D0099106molecular_functionion channel regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 134
ChainResidue
BTYR28
BGLY30
BGLY32
BASP49
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 134
ChainResidue
CTYR28
CGLY30
CGLY32
CASP49
Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCFvHDcC
ChainResidueDetails
BCYS44-CYS51
ACYS44-CYS51
site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICECDRVAaEC
ChainResidueDetails
BILE95-CYS105
AILE95-CYS105
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P62022","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62022","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Responsible for the weak stability and toxicity","evidences":[{"source":"PubMed","id":"21787789","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues38
DetailsSite: {"description":"Putative interfacial binding surface (IBS)","evidences":[{"source":"PubMed","id":"21787789","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Responsible for the reduced anticoagulant activity (compared with CBc)","evidences":[{"source":"PubMed","id":"18062812","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PubMed","id":"18275084","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18275084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QOG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Responsible for the higher anticoagulant activity (compared with CBa2)","evidences":[{"source":"PubMed","id":"18062812","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP99
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
DHIS48
DGLY30
DASP99
site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP99
site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
CHIS48
CGLY30
CASP99

239803

PDB entries from 2025-08-06

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