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1A3D

PHOSPHOLIPASE A2 (PLA2) FROM NAJA NAJA VENOM

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
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0050482biological_processarachidonate secretion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 200
ChainResidue
AHOH292
AHOH292
AHOH292
AASP39
AASP39
AASP39

site_idCAB
Number of Residues6
DetailsCALCIUM BINDING RESIDUES.
ChainResidue
ATYR27
ACYS28
AGLY29
AARG30
AGLY31
AASP48

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCQvHDnC
ChainResidueDetails
ACYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRLAaIC
ChainResidueDetails
AVAL89-CYS99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:8419939
ChainResidueDetails
AHIS47
AASP93

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8419939, ECO:0007744|PDB:1PSH
ChainResidueDetails
ATYR27
AGLY29
AGLY31
AASP48

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS47
AASP93
AGLY29

227344

PDB entries from 2024-11-13

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