Structure of PDB 1bsk Chain A

Receptor sequence
>1bskA (length=166) Species: 562 (Escherichia coli) [Search protein sequence]
SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQ
VDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALV
PRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLK
QQRIRQKVEKLDRLKA
3D structure
PDB1bsk Structural basis for the design of antibiotics targeting peptide deformylase.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A C90 H132 H136 C90 H132 H136
BS02 MLN A G43 I44 G45 Q50 E88 G89 L91 H132 E133 H136 G43 I44 G45 Q50 E88 G89 L91 H132 E133 H136 PDBbind-CN: -logKd/Ki=4.12,Ki=76uM
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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Cellular Component
External links
PDB RCSB:1bsk, PDBe:1bsk, PDBj:1bsk
PDBsum1bsk
PubMed10200158
UniProtP0A6K3|DEF_ECOLI Peptide deformylase (Gene Name=def)

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