› 1def

Solution NMR

PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES

Released:
DOI: 10.2210/pdb1def/pdb
PDB entry 1def coloured by chain, ensemble of 9 models, front view.
PDB entry 1def coloured by chain, ensemble of 9 models, side view.
PDB entry 1def coloured by chain, ensemble of 9 models, top view.
Source organism: Escherichia coli
Primary publication:
A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.
Meinnel T, Blanquet S, Dardel F
J Mol Biol 262 375-86 (1996)
PMID: 8845003

Function and Biology Details

Reaction catalysed: 
Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 16.66 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6K3 (Residues: 2-148; Coverage: 87%)
Gene names: JW3248, b3287, def, fms
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Linkage map of Escherichia coli K-12, edition 10: the traditional map.
Berlyn MK. (1998)
7 more

4 mentions without citation

Prediction of protein structural classes for low-homology sequences based on predicted secondary structure.
Yang et al. (2010)
3 more