› 2fu7

X-ray diffraction
1.85Å resolution

Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (Cu-substituted form)

Released:
DOI: 10.2210/pdb2fu7/pdb
PDB entry 2fu7 coloured by chain, front view.
PDB entry 2fu7 coloured by chain, side view.
PDB entry 2fu7 coloured by chain, top view.
Source organism: Stenotrophomonas maltophilia
Primary publication:
Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
Nauton L, Kahn R, Garau G, Hernandez JF, Dideberg O
J Mol Biol 375 257-69 (2008)
PMID: 17999929

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-156599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase L1 type 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 269 amino acids
Theoretical weight: 28.74 KDa
Source organism: Stenotrophomonas maltophilia
Expression system: Escherichia coli
UniProt:
  • Canonical: P52700 (Residues: 22-290; Coverage: 100%)
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

4 bound ligands:
Ligand CU 6 x CU
Ligand SO4 6 x SO4
Ligand PHN 2 x PHN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P6522
Unit cell:
a: 105.35Å b: 105.35Å c: 196.28Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.195
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

2 mentions without citation

A close look onto structural models and primary ligands of metallo-β-lactamases.
Raczynska et al. (2018)
1 more