7llb

X-ray diffraction
1.67Å resolution

Crystal structure of KPC-2 S70G/T215P mutant with hydrolyzed meropenem

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbapenem-hydrolyzing beta-lactamase KPC Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 27.96 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 26-289; Coverage: 98%)
Gene names: bla, kpc, kpc1
Sequence domains: Beta-lactamase enzyme family

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 34.495Å b: 37.292Å c: 82.128Å
α: 91.391° β: 90.372° γ: 93.789°
R-values:
R R work R free
0.172 0.171 0.193
Expression system: Escherichia coli