PDBe 2b3h

X-ray diffraction
1.1Å resolution

Crystal structure of Human Methionine Aminopeptidase Type I with a third cobalt in the active site

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P53582 (Residues: 81-384; Coverage: 79%)
Gene names: KIAA0094, METAP1
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 47.29Å b: 77.3Å c: 48.34Å
α: 90° β: 91.03° γ: 90°
R-values:
R R work R free
0.101 0.101 0.131
Expression system: Escherichia coli BL21(DE3)