2g6p

X-ray diffraction
1.9Å resolution

Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative

Released:
Source organism: Homo sapiens
Primary publication:
Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases.
Angew Chem Int Ed Engl 45 3772-5 (2006)
PMID: 16724298

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-156814 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 34.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: 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: 47.386Å b: 77.522Å c: 47.72Å
α: 90° β: 90.82° γ: 90°
R-values:
R R work R free
0.193 0.193 0.241
Expression system: Escherichia coli