› 1sml

X-ray diffraction
1.7Å resolution

METALLO BETA LACTAMASE L1 FROM STENOTROPHOMONAS MALTOPHILIA

Released:
DOI: 10.2210/pdb1sml/pdb
PDB entry 1sml coloured by chain, front view.
PDB entry 1sml coloured by chain, side view.
PDB entry 1sml coloured by chain, top view.
Source organism: Stenotrophomonas maltophilia
Primary publication:
The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution.
Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ, Spencer J
J Mol Biol 284 125-36 (1998)
PMID: 9811546

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 Chain: A
Molecule details ›
Chain: A
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

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P6422
Unit cell:
a: 105.23Å b: 105.23Å c: 97.72Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.233
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

37 mentions without citation

Metallo-β-lactamase structure and function.
Palzkill T. (2013)
36 more