Structure of PDB 1i0b Chain B Binding Site BS01

Receptor Information
>1i0b Chain B (length=331) Species: 293 (Brevundimonas diminuta) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKA
VRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFD
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELV
LKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALL
IKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVI
PFLREKGVPQETLAGITVTNPARFLSPTLRA
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1i0b Chain B Residue 401 [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)		H55 H57 D301
Binding residue
(residue number reindexed from 1)		H22 H24 D268
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) H22 H24 K136 H168 H197 D200 H221 D268
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]