› 1bul

X-ray diffraction
1.89Å resolution

6ALPHA-(HYDROXYPROPYL)PENICILLANATE ACYLATED ON NMC-A BETA-LACTAMASE FROM ENTEROBACTER CLOACAE

Released:
DOI: 10.2210/pdb1bul/pdb
PDB entry 1bul coloured by chain, front view.
PDB entry 1bul coloured by chain, side view.
PDB entry 1bul coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
Inhibition of the Nmc-A B-Lactamase by a Penicillanic Acid Derivative, and the Structural Bases for the Increase in Substrate Profile of This Antibiotic Resistance Enzyme
Mourey L, Swaren P, Miyashita K, Bulychev A, Mobashery S, Samama JP
J. Am. Chem. Soc. 120 9382-9383 (1998)

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imipenem-hydrolyzing beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 29.14 KDa
Source organism: Enterobacter cloacae
UniProt:
  • Canonical: P52663 (Residues: 28-292; Coverage: 100%)
Gene name: nmcA
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand AP3 1 x AP3
Ligand MES 3 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P21212
Unit cell:
a: 77.55Å b: 52.46Å c: 67.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.257

Quick links

Citations

4 mentions without citation

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
3 more