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1P7O

Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka

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_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
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
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
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
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
F0046872molecular_functionmetal ion binding
F0047498molecular_functioncalcium-dependent phospholipase A2 activity
F0050482biological_processarachidonic acid 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
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS48
AASP99
BHIS48
BASP99
CHIS48
CASP99
DHIS48
DASP99
EHIS48
EASP99
FHIS48
FASP99

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
EGLY32
EASP49
FTYR28
FGLY30
FGLY32
FASP49
ATYR28
AGLY30
AGLY32
AASP49
BTYR28
BGLY30
BGLY32
BASP49
CTYR28
CGLY30
CGLY32
CASP49
DTYR28
DGLY30
DGLY32
DASP49
ETYR28
EGLY30

220472

PDB entries from 2024-05-29

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