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1OZY

Crystal Structure of Phospholipase A2 (MIPLA3) From Micropechis Ikaheka

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0050482biological_processarachidonate secretion
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0050482biological_processarachidonate secretion
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 122
ChainResidue
AARG6
ALYS7
ALYS10
BLYS92

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 123
ChainResidue
AGLN4
ATHR72
AHOH218
BGLN4

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

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

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

247536

PDB entries from 2026-01-14

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