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:
- Peptidase M24, methionine aminopeptidase
- Creatinase/aminopeptidase-like
- Peptidase M24A, methionine aminopeptidase, subfamily 2
- Winged helix DNA-binding domain superfamily
- Winged helix-like DNA-binding domain superfamily
- Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site
- Peptidase M24
- Methionine aminopeptidase, archaeal
Structure domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Methionine aminopeptidase (preferred)
PDBe Complex ID:
PDB-CPX-157434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 32.89 KDa
Source organism: Pyrococcus furiosus
UniProt:
Sequence domains: Metallopeptidase family M24
Structure domains:
Length: 295 amino acids
Theoretical weight: 32.89 KDa
Source organism: Pyrococcus furiosus
UniProt:
- Canonical:
P56218 (Residues: 1-295; Coverage: 100%)
Sequence domains: Metallopeptidase family M24
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RUH2R
Spacegroup:
P62
