1c22

X-ray diffraction
1.75Å resolution

E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX

Released:

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)
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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 39.128Å b: 67.604Å c: 48.826Å
α: 90° β: 111.05° γ: 90°
R-values:
R R work R free
0.163 not available not available
Expression system: Escherichia coli