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1A2A

AGKISTROTOXIN, A PHOSPHOLIPASE A2-TYPE PRESYNAPTIC NEUROTOXIN FROM AGKISTRODON HALYS PALLAS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionA2-type glycerophospholipase activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0042130biological_processnegative regulation of T cell proliferation
A0050482biological_processarachidonate secretion
B0004623molecular_functionA2-type glycerophospholipase activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0042130biological_processnegative regulation of T cell proliferation
B0050482biological_processarachidonate secretion
C0004623molecular_functionA2-type glycerophospholipase activity
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0042130biological_processnegative regulation of T cell proliferation
C0050482biological_processarachidonate secretion
D0004623molecular_functionA2-type glycerophospholipase activity
D0005509molecular_functioncalcium ion binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
D0006644biological_processphospholipid metabolic process
D0016042biological_processlipid catabolic process
D0042130biological_processnegative regulation of T cell proliferation
D0050482biological_processarachidonate secretion
E0004623molecular_functionA2-type glycerophospholipase activity
E0005509molecular_functioncalcium ion binding
E0005543molecular_functionphospholipid binding
E0005576cellular_componentextracellular region
E0006644biological_processphospholipid metabolic process
E0016042biological_processlipid catabolic process
E0042130biological_processnegative regulation of T cell proliferation
E0050482biological_processarachidonate secretion
F0004623molecular_functionA2-type glycerophospholipase activity
F0005509molecular_functioncalcium ion binding
F0005543molecular_functionphospholipid binding
F0005576cellular_componentextracellular region
F0006644biological_processphospholipid metabolic process
F0016042biological_processlipid catabolic process
F0042130biological_processnegative regulation of T cell proliferation
F0050482biological_processarachidonate secretion
G0004623molecular_functionA2-type glycerophospholipase activity
G0005509molecular_functioncalcium ion binding
G0005543molecular_functionphospholipid binding
G0005576cellular_componentextracellular region
G0006644biological_processphospholipid metabolic process
G0016042biological_processlipid catabolic process
G0042130biological_processnegative regulation of T cell proliferation
G0050482biological_processarachidonate secretion
H0004623molecular_functionA2-type glycerophospholipase activity
H0005509molecular_functioncalcium ion binding
H0005543molecular_functionphospholipid binding
H0005576cellular_componentextracellular region
H0006644biological_processphospholipid metabolic process
H0016042biological_processlipid catabolic process
H0042130biological_processnegative regulation of T cell proliferation
H0050482biological_processarachidonate secretion
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 200
ChainResidue
AARG108
DGLN4
DTYR75

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 400
ChainResidue
CARG108

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL E 600
ChainResidue
EARG108
HGLN4

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL F 800
ChainResidue
FGLN4
FTYR75
GARG108

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCFvHDcC
ChainResidueDetails
ACYS44-CYS51

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9733637","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10666574","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BJJ","evidenceCode":"ECO:0007744"}]}
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
BHIS48
BGLY30
BASP99

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
CHIS48
CGLY30
CASP99

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
DHIS48
DGLY30
DASP99

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
EHIS48
EGLY30
EASP99

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
FHIS48
FGLY30
FASP99

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
GHIS48
GGLY30
GASP99

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
HHIS48
HGLY30
HASP99

251801

PDB entries from 2026-04-08

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