Structure of PDB 2w3t Chain A Binding Site BS02

Receptor Information
>2w3t Chain A (length=167) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQ
VDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALV
PRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLK
QQRIRQKVEKLDRLKAR
Ligand information
Ligand IDCL
InChIInChI=1S/ClH/h1H/p-1
InChIKeyVEXZGXHMUGYJMC-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Cl-]
FormulaCl
NameCHLORIDE ION
ChEMBL
DrugBankDB14547
ZINC
PDB chain2w3t Chain A Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2w3t Structure of the Ni(II) Complex of Escherichia Coli Peptide Deformylase and Suggestions on Deformylase Activities Depending on Different Metal(II) Centres.
Resolution1.69 Å
Binding residue
(original residue number in PDB)		Q50 H132
Binding residue
(residue number reindexed from 1)		Q50 H132
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G45 Q50 C90 L91 H132 E133 H136
Catalytic site (residue number reindexed from 1) G45 Q50 C90 L91 H132 E133 H136
Enzyme Commision number 3.5.1.88: peptide deformylase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008198 ferrous iron binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0042586 peptide deformylase activity
GO:0043022 ribosome binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0043686 co-translational protein modification
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2w3t, PDBe:2w3t, PDBj:2w3t
PDBsum2w3t
PubMed20112455
UniProtP0A6K3|DEF_ECOLI Peptide deformylase (Gene Name=def)

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