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

1OYF

Crystal Structure of Russelles viper (Daboia russellii pulchella) phospholipase A2 in a complex with venom 6-methyl heptanol

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
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0050482biological_processarachidonic acid secretion
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
AASN67
APRO68
AGLN69
ASER70
AHOH3045

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MHN A 1001
ChainResidue
AALA18
ACYS45
AHIS48
AASP49

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MHN B 1002
ChainResidue
BLEU2
BALA18
BTYR22
BCYS45
BHIS48
BASP49

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 3001
ChainResidue
AALA40
AHOH3029

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCFvHDcC
ChainResidueDetails
ACYS44-CYS51
BCYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICECDKAAaIC
ChainResidueDetails
AILE95-CYS105
BILE95-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

PDB statisticsPDBj update infoContact PDBjnumon