5k1d

X-ray diffraction
1.94Å resolution

Crystal structure of a class C beta lactamase/compound1 complex

Released:
Model geometry
Fit model/data
Source organism: Klebsiella aerogenes
Primary publication:
GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C β-Lactamase.
Antimicrob Agents Chemother 61 (2017)
PMID: 28242658

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-189388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase CMY-10 Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 39.3 KDa
Source organism: Klebsiella aerogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99QC1 (Residues: 24-382; Coverage: 100%)
Gene name: blaCMY-10
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P212121
Unit cell:
a: 49.625Å b: 59.381Å c: 112.833Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.244
Expression system: Escherichia coli