Structure of PDB 2o4q Chain P Binding Site BS02

Receptor Information

>2o4q Chain P (length=330) Species: 293 (Brevundimonas diminuta)

GDRINTVRGPITISEAGFTLTHEHICASSAGFLRAWPEFFGSRKALAEKA
VRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFD
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELV
LKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALL
IKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVI
PFLREKGVPQETLAGITVTNPARFLSPTLR

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2o4q Chain P Residue 2408

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2o4q Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase.
• Resolution: 1.95 Å
• Binding residue (original residue number in PDB): K169 H201 H230
• Binding residue (residue number reindexed from 1): K136 H168 H197
• Annotation score: 1

Enzymatic activity

• 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

External links

• PDB: RCSB:2o4q, PDBe:2o4q, PDBj:2o4q
• PDBsum: 2o4q
• PubMed: 18702530
• UniProt: P0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)