Structure of PDB 1i0b Chain A Binding Site BS03

Receptor Information
>1i0b Chain A (length=331) Species: 293 (Brevundimonas diminuta) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
KAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLI
KALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIP
FLREKGVPQETLAGITVTNPARFLSPTLRAS
Ligand information
Ligand IDPEL
InChIInChI=1S/C8H10O/c9-7-6-8-4-2-1-3-5-8/h1-5,9H,6-7H2
InChIKeyWRMNZCZEMHIOCP-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(cc1)CCO
ACDLabs 10.04
CACTVS 3.341		OCCc1ccccc1
FormulaC8 H10 O
Name2-PHENYL-ETHANOL
ChEMBLCHEMBL448500
DrugBankDB02192
ZINCZINC000000895934
PDB chain1i0b Chain A Residue 434 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1i0b High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		M293 K294 G348 I349 N353
Binding residue
(residue number reindexed from 1)		M259 K260 G314 I315 N319
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H55 H57 K169 H201 H230 D233 H254 D301
Catalytic site (residue number reindexed from 1) H21 H23 K135 H167 H196 D199 H220 D267
Enzyme Commision number 3.1.8.1: aryldialkylphosphatase.
Gene Ontology
Molecular Function
GO:0004063 aryldialkylphosphatase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
Cellular Component
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1i0b, PDBe:1i0b, PDBj:1i0b
PDBsum1i0b
PubMed11258882
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

[Back to BioLiP]