6uaf

X-ray diffraction
1.9Å resolution

Crystal Structure of the Metallo-beta-lactamase L1 from Stenotrophomonas maltophilia in the Complex with Hydrolyzed Imipnem

Released:
Entry authors: Kim Y, Maltseva N, Endres M, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactamase_B domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 31.17 KDa
Source organism: Stenotrophomonas maltophilia K279a
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B2FTM1 (Residues: 1-290; Coverage: 100%)
Gene name: Smlt2667
Sequence domains: Metallo-beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P6422
Unit cell:
a: 104.835Å b: 104.835Å c: 98.627Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.172 0.208
Expression system: Escherichia coli BL21(DE3)