› 2p98

X-ray diffraction
1.7Å resolution

E. coli methionine aminopeptidase monometalated with inhibitor YE7

Released:
DOI: 10.2210/pdb2p98/pdb
PDB entry 2p98 coloured by chain, front view.
PDB entry 2p98 coloured by chain, side view.
PDB entry 2p98 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis.
Huang M, Xie SX, Ma ZQ, Huang QQ, Nan FJ, Ye QZ
J Med Chem 50 5735-42 (2007)
PMID: 17948983

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 29.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AE18 (Residues: 2-263; Coverage: 99%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
Ligand MN 1 x MN
Ligand NA 1 x NA
Ligand YE7 1 x YE7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, null
Spacegroup: P21
Unit cell:
a: 38.19Å b: 60.27Å c: 50.61Å
α: 90° β: 104.59° γ: 90°
R-values:
R R work R free
0.207 0.207 0.238
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Metallo-aminopeptidase inhibitors.
Mucha et al. (2010)
1 more

1 mention without citation

Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis.
Huang et al. (2007)