› 2qin

X-ray diffraction
1.76Å resolution

Stenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutant

Released:
DOI: 10.2210/pdb2qin/pdb
PDB entry 2qin coloured by chain, front view.
PDB entry 2qin coloured by chain, side view.
PDB entry 2qin coloured by chain, top view.
Source organism: Stenotrophomonas maltophilia
Primary publication:
Structural basis for the role of Asp-120 in metallo-beta-lactamases.
Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J
Biochemistry 46 10664-74 (2007)
PMID: 17715946

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:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase L1 type 3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 269 amino acids
Theoretical weight: 28.73 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

2 bound ligands:
Ligand ZN 9 x ZN
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 66.141Å b: 112.845Å c: 78.352Å
α: 90° β: 113.35° γ: 90°
R-values:
R R work R free
0.175 0.173 0.212
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Overcoming differences: The catalytic mechanism of metallo-β-lactamases.
Meini et al. (2015)
4 more

2 mentions without citation

Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?
Oelschlaeger et al. (2010)
1 more