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1SXK

Crystal Structure of a complex formed between phospholipase A2 and a non-specific anti-inflammatory amino salicylic acid at 1.2 A 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
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ASER114
ALYS115
ALYS131
AHOH443

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHOH433
AHOH499
AASN54
APRO56
AARG94
AHOH323
AHOH413

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AASP39
AARG43
AHOH470
AHOH480
AHOH486

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AGLU4
AARG72
ALYS74
AHOH361
AHOH378
AHOH388
AHOH402
AHOH500

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BHA A 251
ChainResidue
AILE19
APRO20
ALYS74
AGLN108
AASN111
AHOH339
AHOH358
AHOH400
AHOH435
AHOH472

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP99

227111

PDB entries from 2024-11-06

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