› 4f6z

X-ray diffraction
2Å resolution

Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-b-lactamase active site

Released:
DOI: 10.2210/pdb4f6z/pdb
PDB entry 4f6z coloured by chain, front view.
PDB entry 4f6z coloured by chain, side view.
PDB entry 4f6z coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-β-lactamase active site.
Horton LB, Shanker S, Mikulski R, Brown NG, Phillips KJ, Lykissa E, Venkataram Prasad BV, Palzkill T
Antimicrob Agents Chemother 56 5667-77 (2012)
PMID: 22908171

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-565432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 26.14 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q79MP6 (Residues: 19-246; Coverage: 100%)
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 1 x ZN
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 50.031Å b: 59.774Å c: 83.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.249
Expression system: Escherichia coli

Quick links

Citations

3 review citations

B1-Metallo-β-Lactamases: Where Do We Stand?
Mojica et al. (2016)
2 more

1 mention without citation

Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-β-lactamase active site.
Horton et al. (2012)