Structure of PDB 1lru Chain A

Receptor sequence
>1lruA (length=164) Species: 562 (Escherichia coli) [Search protein sequence]
SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQ
VDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALV
PRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLK
QQRIRQKVEKLDRL
3D structure
PDB1lru The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 BB2 A G43 I44 G45 Q50 E87 G89 C90 L91 R97 H132 E133 H136 G43 I44 G45 Q50 E87 G89 C90 L91 R97 H132 E133 H136
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1lru, PDBe:1lru, PDBj:1lru
PDBsum1lru
PubMed12126617
UniProtP0A6K3|DEF_ECOLI Peptide deformylase (Gene Name=def)

[Back to BioLiP]