2evm

X-ray diffraction
1.7Å resolution

crystal structure of methionine aminopeptidase in complex with 5-(2,5-dichlorophenyl)furan-2-carboxylic acid

Released:
Source organism: Escherichia coli
Primary publication:
Structural analysis of metalloform-selective inhibition of methionine aminopeptidase.
Acta Crystallogr D Biol Crystallogr 62 425-32 (2006)
PMID: 16552144

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 29.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE18 (Residues: 1-264; Coverage: 100%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 37.8Å b: 60.2Å c: 50.4Å
α: 90° β: 104.5° γ: 90°
R-values:
R R work R free
0.232 0.215 0.248
Expression system: Escherichia coli