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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
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_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
A0099106molecular_functionion channel regulator activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0042130biological_processnegative regulation of T cell proliferation
B0044398biological_processenvenomation resulting in induction of edema in another organism
B0044478biological_processenvenomation resulting in positive regulation of platelet aggregation in another organism
B0044521biological_processenvenomation resulting in muscle damage in another organism
B0044522biological_processenvenomation resulting in myocyte killing in another organism
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0090729molecular_functiontoxin activity
B0099106molecular_functionion channel regulator activity
C0004623molecular_functionphospholipase A2 activity
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0016787molecular_functionhydrolase activity
C0042130biological_processnegative regulation of T cell proliferation
C0044398biological_processenvenomation resulting in induction of edema in another organism
C0044478biological_processenvenomation resulting in positive regulation of platelet aggregation in another organism
C0044521biological_processenvenomation resulting in muscle damage in another organism
C0044522biological_processenvenomation resulting in myocyte killing in another organism
C0046872molecular_functionmetal ion binding
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonic acid secretion
C0090729molecular_functiontoxin activity
C0099106molecular_functionion channel regulator activity
D0004623molecular_functionphospholipase A2 activity
D0005509molecular_functioncalcium ion binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
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_processarachidonic acid 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
ACYS44-CYS51
BCYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICECDRVAaEC
ChainResidueDetails
AILE95-CYS105
BILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:18275084
ChainResidueDetails
BHIS48
BASP99
CHIS48
CASP99

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18275084, ECO:0007744|PDB:2QOG
ChainResidueDetails
BTYR28
BGLY30
BGLY32
BASP49
CTYR28
CGLY30
CGLY32
CASP49

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Responsible for the weak stability and toxicity => ECO:0000269|PubMed:21787789
ChainResidueDetails
BHIS1
CHIS1

site_idSWS_FT_FI4
Number of Residues18
DetailsSITE: Putative interfacial binding surface (IBS) => ECO:0000269|PubMed:21787789
ChainResidueDetails
BLEU2
CLEU2
CLEU3
CLYS7
CLYS10
CALA18
CALA23
CPHE24
CLYS69
CTYR113
DLYS69
BLEU3
DTYR113
BLYS7
BLYS10
BALA18
BALA23
BPHE24
BLYS69
BTYR113

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Responsible for the higher anticoagulant activity (compared with CBa2) => ECO:0000269|PubMed:18062812
ChainResidueDetails
BGLY128
CGLY128

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

225158

PDB entries from 2024-09-18

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