3mx6

X-ray diffraction
1.7Å resolution

Crystal structure of methionine aminopeptidase from Rickettsia prowazekii bound to methionine

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-579198 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 29.1 KDa
Source organism: Rickettsia prowazekii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZCD3 (Residues: 3-259; Coverage: 99%)
Gene names: RP824, 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: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 50.37Å b: 67.55Å c: 80.89Å
α: 90° β: 97.43° γ: 90°
R-values:
R R work R free
0.169 0.168 0.207
Expression system: Escherichia coli