› 5hh4

X-ray diffraction
2Å resolution

Crystal structure of metallo-beta-lactamase IMP-1 in complex with a phosphonate-based inhibitor

Released:
DOI: 10.2210/pdb5hh4/pdb
PDB entry 5hh4 coloured by chain, front view.
PDB entry 5hh4 coloured by chain, side view.
PDB entry 5hh4 coloured by chain, top view.
Source organism: Serratia marcescens
Primary publication:
Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.
Hinchliffe P, Tanner CA, Krismanich AP, Labbé G, Goodfellow VJ, Marrone L, Desoky AY, Calvopiña K, Whittle EE, Zeng F, Avison MB, Bols NC, Siemann S, Spencer J, Dmitrienko GI
OpenAccess logo Biochemistry 57 1880-1892 (2018)
PMID: 29485857

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-156597 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 230 amino acids
Theoretical weight: 25.29 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P52699 (Residues: 19-246; Coverage: 100%)
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

4 bound ligands:
Ligand ZN 8 x ZN
Ligand 60M 2 x 60M
Ligand CL 1 x CL
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 48.943Å b: 78.309Å c: 260.545Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
7 more

5 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
4 more