› 1c21

X-ray diffraction
1.8Å resolution

E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE COMPLEX

Released:
DOI: 10.2210/pdb1c21/pdb
PDB entry 1c21 coloured by chain, front view.
PDB entry 1c21 coloured by chain, side view.
PDB entry 1c21 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW
Biochemistry 38 14810-9 (1999)
PMID: 10555963

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: 263 amino acids
Theoretical weight: 29.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE18 (Residues: 2-264; Coverage: 100%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
Ligand CO 2 x CO
Ligand NA 1 x NA
Ligand MET 1 x MET
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 39.242Å b: 67.588Å c: 48.927Å
α: 90° β: 111.2° γ: 90°
R-values:
R R work R free
0.163 not available not available
Expression system: Escherichia coli

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Citations

1 review citation

Protein-reactive natural products.
Drahl et al. (2005)
39 other articles

6 mentions without citation

Functional diversity and electron donor dependence of microbial populations capable of U(VI) reduction in radionuclide-contaminated subsurface sediments.
Akob et al. (2008)
5 more