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1PSH

CRYSTAL STRUCTURE OF PHOSPHOLIPASE A2 FROM INDIAN COBRA REVEALS A TRIMERIC ASSOCIATION

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
A0050482biological_processarachidonate secretion
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
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonate secretion
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
C0046872molecular_functionmetal ion binding
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonate secretion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 120
ChainResidue
ATYR27
AGLY29
AGLY31
AASP48
AHOH130
AHOH144

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 120
ChainResidue
BASP48
BHOH147
BTYR27
BGLY29
BGLY31

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 120
ChainResidue
CTYR27
CGLY29
CGLY31
CASP48
CHOH132
CHOH134

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 Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:8419939
ChainResidueDetails
AHIS47
AASP93
BHIS47
BASP93
CHIS47
CASP93

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:8419939, ECO:0007744|PDB:1PSH
ChainResidueDetails
ATYR27
CGLY29
CGLY31
CASP48
AGLY29
AGLY31
AASP48
BTYR27
BGLY29
BGLY31
BASP48
CTYR27

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS47
BASP93
BGLY29

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
CHIS47
CASP93
CGLY29

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PDB entries from 2024-09-25

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