› 2ea4

X-ray diffraction
2.35Å 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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156226 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase 2 Chain: A
Molecule details ›
Chain: A
Length: 369 amino acids
Theoretical weight: 41.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50579 (Residues: 110-478; Coverage: 77%)
Gene names: METAP2, MNPEP, P67EIF2
Sequence domains: Metallopeptidase family M24
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand F79 1 x F79
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2221
Unit cell:
a: 90.091Å b: 100.28Å c: 100.722Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.211 0.272
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Metallo-aminopeptidase inhibitors.
Mucha et al. (2010)
7 other articles

1 mention without citation

Redox regulation of methionine aminopeptidase 2 activity.
Chiu et al. (2014)