› 8oxg

X-ray diffraction
1.73Å resolution

Crystal structure of human methionine aminopeptidase-2 complexed with (3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-2-buten-1-yl)-2-oxiranyl]-1-oxaspiro[2.5]oct-6-yl N-(trans-4-aminocyclohexyl)carbamate

Released:
DOI: 10.2210/pdb8oxg/pdb
PDB entry 8oxg coloured by chain, front view.
PDB entry 8oxg coloured by chain, side view.
PDB entry 8oxg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pharmacological Characterization of SDX-7320/Evexomostat: a Novel Methionine Aminopeptidase Type 2 Inhibitor with Anti-Tumor and Anti-Metastatic Activity.
Cornelius P, Mayes BA, Petersen JS, Turnquist DJ, Dufour PJ, Dannenberg AJ, Shanahan JM, Carver BJ
OpenAccess logo Mol Cancer Ther (2024)
PMID: 38530115

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-242877 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 384 amino acids
Theoretical weight: 43.27 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P50579 (Residues: 108-478; Coverage: 78%)
Gene names: METAP2, MNPEP, P67EIF2
Sequence domains: Metallopeptidase family M24

Ligands and Environments

2 bound ligands:
Ligand W5N 2 x W5N
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 119.05Å b: 101.127Å c: 83.737Å
α: 90° β: 98.755° γ: 90°
R-values:
R R work R free
0.183 0.181 0.215
Expression system: Spodoptera frugiperda

Quick links

Citations

1 mention without citation

Inosine, but none of the 8-oxo-purines, is a plausible component of a primordial version of RNA.
Kim et al. (2018)