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1Q7A

Crystal structure of the complex formed between russell's viper phospholipase A2 and an antiinflammatory agent oxyphenbutazone at 1.6A 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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 122
ChainResidue
ALYS15
ALYS67
AHOH167
AHOH206
AHOH233

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 123
ChainResidue
ASER1
ALEU3
AARG63

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OPB A 124
ChainResidue
APHE5
AGLY6
AALA17
AGLY29
ATRP30
AHIS47
ATYR51
ALYS60
AASN101
AMOH125
AHOH153
ALEU2

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MOH A 125
ChainResidue
ATYR27
ACYS28
AGLY29
ACYS44
AOPB124
AHOH234

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCFvHDcC
ChainResidueDetails
ACYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICECDKAAaIC
ChainResidueDetails
AILE85-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P14418
ChainResidueDetails
AHIS47
AASP89

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM
ChainResidueDetails
ATYR27
AGLY29
AGLY31
AASP48

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS47
AASP89
AGLY29

219140

PDB entries from 2024-05-01

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