Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TG1

Crystal Structure of the complex formed between russells viper phospholipase A2 and a designed peptide inhibitor PHQ-Leu-Val-Arg-Tyr at 1.2A 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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG43
AHOH401
AHOH414
CPHQ1

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHOH389
AHOH418
AGLU4
AARG72
ALYS74
AHOH374
AHOH383

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ASER114
ALYS115
ALYS131
AHOH497

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 304
ChainResidue
ALYS38
ATYR117
AHOH410

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR CHAIN C OF PEPTIDE INHIBITOR
ChainResidue
ALEU2
ALEU3
AILE19
ATYR22
ASER23
ATYR28
ACYS29
AGLY30
ATRP31
AGLY32
ACYS45
AHIS48
AASP49
ATYR52
AASN111
ATHR112
ASO4301
AHOH400
AHOH402
AHOH417
AHOH438
AHOH470
AHOH480
CHOH185
CHOH206
CHOH207

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon