› 3d27

X-ray diffraction
2.2Å resolution

E. coli methionine aminopeptidase with Fe inhibitor W29

Released:
DOI: 10.2210/pdb3d27/pdb
PDB entry 3d27 coloured by chain, front view.
PDB entry 3d27 coloured by chain, side view.
PDB entry 3d27 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity.
Wang WL, Chai SC, Huang M, He HZ, Hurley TD, Ye QZ
J Med Chem 51 6110-20 (2008)
PMID: 18785729

Function and Biology Details

Reaction catalysed: 
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.06 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE18 (Residues: 4-264; Coverage: 99%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand W29 1 x W29
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 38.51Å b: 59.88Å c: 54.88Å
α: 90° β: 106.47° γ: 90°
R-values:
R R work R free
0.193 0.191 0.244
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Challenges of antibacterial discovery.
Silver LL. (2011)
4 more

5 mentions without citation

Emerging trends in metalloprotein inhibition.
Rouffet et al. (2011)
4 more