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1P7O

Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0048146biological_processpositive regulation of fibroblast proliferation
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
B0004623molecular_functionphospholipase A2 activity
B0005102molecular_functionsignaling receptor binding
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0035821biological_processmodulation of process of another organism
B0046872molecular_functionmetal ion binding
B0048146biological_processpositive regulation of fibroblast proliferation
B0050482biological_processarachidonate secretion
B0090729molecular_functiontoxin activity
C0004623molecular_functionphospholipase A2 activity
C0005102molecular_functionsignaling receptor binding
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006629biological_processlipid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0016787molecular_functionhydrolase activity
C0035821biological_processmodulation of process of another organism
C0046872molecular_functionmetal ion binding
C0048146biological_processpositive regulation of fibroblast proliferation
C0050482biological_processarachidonate secretion
C0090729molecular_functiontoxin activity
D0004623molecular_functionphospholipase A2 activity
D0005102molecular_functionsignaling receptor binding
D0005509molecular_functioncalcium ion binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
D0006629biological_processlipid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0006644biological_processphospholipid metabolic process
D0016042biological_processlipid catabolic process
D0016787molecular_functionhydrolase activity
D0035821biological_processmodulation of process of another organism
D0046872molecular_functionmetal ion binding
D0048146biological_processpositive regulation of fibroblast proliferation
D0050482biological_processarachidonate secretion
D0090729molecular_functiontoxin activity
E0004623molecular_functionphospholipase A2 activity
E0005102molecular_functionsignaling receptor binding
E0005509molecular_functioncalcium ion binding
E0005543molecular_functionphospholipid binding
E0005576cellular_componentextracellular region
E0006629biological_processlipid metabolic process
E0006633biological_processfatty acid biosynthetic process
E0006644biological_processphospholipid metabolic process
E0016042biological_processlipid catabolic process
E0016787molecular_functionhydrolase activity
E0035821biological_processmodulation of process of another organism
E0046872molecular_functionmetal ion binding
E0048146biological_processpositive regulation of fibroblast proliferation
E0050482biological_processarachidonate secretion
E0090729molecular_functiontoxin activity
F0004623molecular_functionphospholipase A2 activity
F0005102molecular_functionsignaling receptor binding
F0005509molecular_functioncalcium ion binding
F0005543molecular_functionphospholipid binding
F0005576cellular_componentextracellular region
F0006629biological_processlipid metabolic process
F0006633biological_processfatty acid biosynthetic process
F0006644biological_processphospholipid metabolic process
F0016042biological_processlipid catabolic process
F0016787molecular_functionhydrolase activity
F0035821biological_processmodulation of process of another organism
F0046872molecular_functionmetal ion binding
F0048146biological_processpositive regulation of fibroblast proliferation
F0050482biological_processarachidonate secretion
F0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCQtHDnC
ChainResidueDetails
ACYS44-CYS51

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
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

247947

PDB entries from 2026-01-21

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