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1SZ8

Crystal Structure of an Acidic Phospholipase A2 from Naja Naja Sagittifera at 1.5 A resolution

Replaces:  1LFF
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
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 201
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AACY401
AHOH526

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 301
ChainResidue
ALYS66
ATHR67
AGLN74
AHOH422
AHOH503
AHOH504
AGLU54
AASN57
AARG62

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A 401
ChainResidue
ATYR28
AGLY30
AHIS48
AASP49
ACA201
AHOH481
AHOH525

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:15823962
ChainResidueDetails
AHIS48
AASP94

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15823962, ECO:0007744|PDB:1OXR
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

218853

数据于2024-04-24公开中

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