› 1ddk

X-ray diffraction
3.1Å resolution

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 24.33 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q79MP6 (Residues: 20-239; Coverage: 97%)
Gene names: bla IMP, bla-imp, blaESP, blaIMP-1, imp
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 50.3Å b: 105.8Å c: 112.3Å
α: 90° β: 93.9° γ: 90°
R-values:
R R work R free
0.255 0.255 0.288
Expression system: Escherichia coli BL21

Quick links

Citations

30 review citations

Carbapenemases: the versatile beta-lactamases.
Queenan et al. (2007)
29 more

24 mentions without citation

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