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1SQZ

Design of specific inhibitors of Phopholipase A2: Crystal structure of the complex formed between Group II Phopholipase A2 and a designed peptide Dehydro-Ile-Ala-Arg-Ser at 1.2A 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
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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG43
AHOH318
AHOH360
AHOH393
AHOH449
BPHQ1

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHOH423
AHOH512
AHOH530
ASER114
ALYS115
ALYS131

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AGLU4
AARG72
ALYS74
AHOH347
AHOH352
AHOH355
AHOH366
AHOH372
AHOH397
AHOH442
AHOH448

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR CHAIN B OF SYNTHETIC PEPTIDE
ChainResidue
ALEU2
AGLY30
ATRP31
AHIS48
AASP49
ATYR52
ALYS69
AASN111
ATHR112
ASO4301
AHOH404
AHOH571

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

218853

PDB entries from 2024-04-24

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