2bb7

X-ray diffraction
1.7Å resolution

Mn Form Of E. coli Methionine Aminopeptidase In Complex With a quinolinyl sulfonamide inhibitor

Released:
Source organism: Escherichia coli
Primary publication:
Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides.
Biochem Biophys Res Commun 339 506-13 (2006)
PMID: 16300729

Function and Biology Details

Reaction catalysed:
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 29.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AE18 (Residues: 1-264; Coverage: 100%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 38.039Å b: 60.416Å c: 50.521Å
α: 90° β: 104.4° γ: 90°
R-values:
R R work R free
0.19 0.187 0.233
Expression system: Escherichia coli BL21(DE3)