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1PSJ

ACIDIC PHOSPHOLIPASE A2 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
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 200
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH212

site_idCAL
Number of Residues4
DetailsTHE CALCIUM ION IS COORDINATED TO THE TWO CARBOXYLATE OXYGENS OF ASP 49 AND EACH CARBONYL OXYGENS OF TYR 28, GLY 30 AND GLY 32 AS WELL AS TWO WATER MOLECULES (HOH 212 AND HOH 213). THESE LIGAND ATOMS FORM A DISTORTED PENTAGONAL BIPYRAMID STRUCTURE. THE AVERAGE DISTANCE OF CALCIUM ION TO LIGANDS OF PROTEIN OXYGEN IS 2.4 ANGSTROMS.
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49

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. ICECDRAAaIC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P06859
ChainResidueDetails
AHIS48
AASP99

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8636969, ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9, ECO:0007744|PDB:1PSJ
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP99

226262

PDB entries from 2024-10-16

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