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1G0Z

SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 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
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonate 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
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonate secretion
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 121
ChainResidue
BTHR82
BSER83
BHOH186

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 121
ChainResidue
ATHR82
ASER83
AHOH167

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICDCDRTAaIC
ChainResidueDetails
AILE90-CYS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15721580","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP94

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP94

239492

PDB entries from 2025-07-30

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