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1XXW

Structure of zinc induced heterodimer of two calcium free isoforms of phospholipase A2 from Naja naja sagittifera at 2.7A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0050482biological_processarachidonate secretion
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
B0046872molecular_functionmetal ion binding
B0048146biological_processpositive regulation of fibroblast proliferation
B0050482biological_processarachidonate secretion
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AASP24
AASN112
AHOH303
AHOH350
BASP24

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 301
ChainResidue
AHOH391

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 302
ChainResidue
BARG31
AHIS48
AASP49
ALYS64

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCQvHDnC
ChainResidueDetails
ACYS44-CYS51
BCYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRLAaIC
ChainResidueDetails
AVAL90-CYS100
BVAL90-CYS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15828003","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S6B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP94

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP94

247947

PDB entries from 2026-01-21

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