Structure of PDB 1dpm Chain A Binding Site BS04

Receptor Information
>1dpm Chain A (length=329) Species: 293 (Brevundimonas diminuta) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
KAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLI
KALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIP
FLREKGVPQETLAGITVTNPARFLSPTLR
Ligand information
Ligand IDEBP
InChIInChI=1S/C12H19O3P/c1-4-14-16(13,15-5-2)10-12-8-6-11(3)7-9-12/h6-9H,4-5,10H2,1-3H3
InChIKeyQKGBKPZAXXBLJE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(OCC)(OCC)Cc1ccc(cc1)C
CACTVS 3.341CCO[P](=O)(Cc1ccc(C)cc1)OCC
OpenEye OEToolkits 1.5.0CCOP(=O)(Cc1ccc(cc1)C)OCC
FormulaC12 H19 O3 P
NameDIETHYL 4-METHYLBENZYLPHOSPHONATE
ChEMBL
DrugBankDB02138
ZINCZINC000002046934
PDB chain1dpm Chain A Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1dpm Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		L151 R152 Q155 Y156
Binding residue
(residue number reindexed from 1)		L117 R118 Q121 Y122
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dpm, PDBe:1dpm, PDBj:1dpm
PDBsum1dpm
PubMed8634243
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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