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1SV3

Structure of the complex formed between Phospholipase A2 and 4-methoxybenzoic acid at 1.3A resolution.

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
A0042130biological_processnegative regulation of T cell proliferation
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 342
ChainResidue
AGLU4
AARG72
ALYS74
AHOH361
AHOH363
AHOH405
AHOH441
AHOH494
AHOH525

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 343
ChainResidue
AARG43
AHOH422
AHOH467
AHOH522

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 344
ChainResidue
ATYR113
ASER114
ALYS115
ALYS131
AHOH526

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 345
ChainResidue
AALA81
ALYS86
ALYS100
ASO4346
AHOH357
AHOH456
AHOH475

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 346
ChainResidue
ALYS86
ASER90
AASN93
ASO4345

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ANN A 347
ChainResidue
ALEU2
ATYR22
AGLY30
APHE106
AHOH511
AHOH548
AHOH554

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. ICECDKAAaIC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P14418
ChainResidueDetails
AHIS48
AASP99

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

219869

PDB entries from 2024-05-15

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