5evl

X-ray diffraction
1.52Å resolution

Crystal Structure of Beta-Lactamase/D-Alanine Carboxypeptidase from Chromobacterium violaceum

Released:
Entry authors: Kim Y, Hatzos-Skintges C, Endres M, Babnigg G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 373 amino acids
Theoretical weight: 40.56 KDa
Source organism: Chromobacterium violaceum ATCC 12472
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7NYG4 (Residues: 26-396; Coverage: 100%)
Gene names: CV_1310, ampC
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 45.604Å b: 59.262Å c: 59.267Å
α: 90° β: 98.18° γ: 90°
R-values:
R R work R free
0.146 0.144 0.182
Expression system: Escherichia coli BL21