› 1o0x

X-ray diffraction
1.9Å resolution

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-194808 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 28.99 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1I7 (Residues: 1-250; Coverage: 100%)
Gene names: TM_1478, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P43212
Unit cell:
a: 62.58Å b: 62.58Å c: 146.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.254
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
6 other articles

4 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
3 more