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1A2A

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

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
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
B0035821biological_processmodulation of process of another organism
B0042130biological_processnegative regulation of T cell proliferation
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0090729molecular_functiontoxin 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
C0035821biological_processmodulation of process of another organism
C0042130biological_processnegative regulation of T cell proliferation
C0046872molecular_functionmetal ion binding
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonic acid secretion
C0090729molecular_functiontoxin 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
E0004623molecular_functionphospholipase A2 activity
E0005509molecular_functioncalcium ion binding
E0005543molecular_functionphospholipid binding
E0005576cellular_componentextracellular region
E0006644biological_processphospholipid metabolic process
E0016042biological_processlipid catabolic process
E0016787molecular_functionhydrolase activity
E0035821biological_processmodulation of process of another organism
E0042130biological_processnegative regulation of T cell proliferation
E0046872molecular_functionmetal ion binding
E0047498molecular_functioncalcium-dependent phospholipase A2 activity
E0050482biological_processarachidonic acid secretion
E0090729molecular_functiontoxin activity
F0004623molecular_functionphospholipase A2 activity
F0005509molecular_functioncalcium ion binding
F0005543molecular_functionphospholipid binding
F0005576cellular_componentextracellular region
F0006644biological_processphospholipid metabolic process
F0016042biological_processlipid catabolic process
F0016787molecular_functionhydrolase activity
F0035821biological_processmodulation of process of another organism
F0042130biological_processnegative regulation of T cell proliferation
F0046872molecular_functionmetal ion binding
F0047498molecular_functioncalcium-dependent phospholipase A2 activity
F0050482biological_processarachidonic acid secretion
F0090729molecular_functiontoxin activity
G0004623molecular_functionphospholipase A2 activity
G0005509molecular_functioncalcium ion binding
G0005543molecular_functionphospholipid binding
G0005576cellular_componentextracellular region
G0006644biological_processphospholipid metabolic process
G0016042biological_processlipid catabolic process
G0016787molecular_functionhydrolase activity
G0035821biological_processmodulation of process of another organism
G0042130biological_processnegative regulation of T cell proliferation
G0046872molecular_functionmetal ion binding
G0047498molecular_functioncalcium-dependent phospholipase A2 activity
G0050482biological_processarachidonic acid secretion
G0090729molecular_functiontoxin activity
H0004623molecular_functionphospholipase A2 activity
H0005509molecular_functioncalcium ion binding
H0005543molecular_functionphospholipid binding
H0005576cellular_componentextracellular region
H0006644biological_processphospholipid metabolic process
H0016042biological_processlipid catabolic process
H0016787molecular_functionhydrolase activity
H0035821biological_processmodulation of process of another organism
H0042130biological_processnegative regulation of T cell proliferation
H0046872molecular_functionmetal ion binding
H0047498molecular_functioncalcium-dependent phospholipase A2 activity
H0050482biological_processarachidonic acid secretion
H0090729molecular_functiontoxin activity
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
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:9733637
ChainResidueDetails
AHIS48
EASP99
FHIS48
FASP99
GHIS48
GASP99
HHIS48
HASP99
AASP99
BHIS48
BASP99
CHIS48
CASP99
DHIS48
DASP99
EHIS48

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ
ChainResidueDetails
ATYR28
CGLY30
CGLY32
CASP49
DTYR28
DGLY30
DGLY32
DASP49
ETYR28
EGLY30
EGLY32
AGLY30
EASP49
FTYR28
FGLY30
FGLY32
FASP49
GTYR28
GGLY30
GGLY32
GASP49
HTYR28
AGLY32
HGLY30
HGLY32
HASP49
AASP49
BTYR28
BGLY30
BGLY32
BASP49
CTYR28

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

219140

PDB entries from 2024-05-01

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