› 2q92

X-ray diffraction
1.9Å resolution

E. coli methionine aminopeptidase Mn-form with inhibitor B23

Released:
DOI: 10.2210/pdb2q92/pdb
PDB entry 2q92 coloured by chain, front view.
PDB entry 2q92 coloured by chain, side view.
PDB entry 2q92 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes.
Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ
BMC Struct Biol 7 84 (2007)
PMID: 18093325

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: 262 amino acids
Theoretical weight: 29.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AE18 (Residues: 2-263; Coverage: 99%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
Ligand MN 2 x MN
Ligand NA 1 x NA
Ligand B23 1 x B23
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 38.137Å b: 60.984Å c: 50.693Å
α: 90° β: 104.93° γ: 90°
R-values:
R R work R free
0.203 0.203 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 mentions without citation

Advances in Bacterial Methionine Aminopeptidase Inhibition.
Helgren et al. (2016)
3 more