› 8g2r

X-ray diffraction
1.28Å resolution

CRYSTAL STRUCTURE OF THE KPC-2 D179N VARIANT IN COMPLEX WITH AVIBACTAM

Released:
DOI: 10.2210/pdb8g2r/pdb
Model geometry
Fit model/data
PDB entry 8g2r coloured by chain, front view.
PDB entry 8g2r coloured by chain, side view.
PDB entry 8g2r coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Exploring avibactam and relebactam inhibition of Klebsiella pneumoniae carbapenemase D179N variant: role of the Ω loop-held deacylation water.
Alsenani TA, Viviani SL, Papp-Wallace KM, Bonomo RA, van den Akker F
Antimicrob Agents Chemother e0035023 (2023)
PMID: 37750722

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbapenem-hydrolyzing beta-lactamase KPC-2 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 28.18 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 24-289; Coverage: 99%)
Gene names: KPC-1, KPC-2, bla, kpc, kpc1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand NXL 1 x NXL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P212121
Unit cell:
a: 51.454Å b: 66.673Å c: 72.435Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.204
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Approaches to Testing Novel β-Lactam and β-Lactam Combination Agents in the Clinical Laboratory.
Russo et al. (2023)
1 other article

1 mention without citation

Exploring avibactam and relebactam inhibition of Klebsiella pneumoniae carbapenemase D179N variant: role of the Ω loop-held deacylation water.
Alsenani et al. (2023)