› 7kis

X-ray diffraction
2.87Å resolution

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194951 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan D,D-transpeptidase MrdA Chains: A, B
Molecule details ›
Chains: A, B
Length: 646 amino acids
Theoretical weight: 72.31 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X6V3 (Residues: 1-646; Coverage: 100%)
Gene names: CAZ10_26315, GNQ48_15490, GUL26_00100, IPC1295_14660, IPC737_17705, L4V69_08310, PAERUG_P19_London_7_VIM_2_05_10_06701, mrdA, pbpA, spoVD
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand C9D 2 x C9D
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X17B1
Spacegroup: P21
Unit cell:
a: 82.018Å b: 75.924Å c: 97.299Å
α: 90° β: 106.73° γ: 90°
R-values:
R R work R free
0.261 0.258 0.316
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Analysis of the Clinical Pipeline of Treatments for Drug-Resistant Bacterial Infections: Despite Progress, More Action Is Needed.
Butler et al. (2022)
5 more

3 mentions without citation

Structural Characterization of Diazabicyclooctane β-Lactam "Enhancers" in Complex with Penicillin-Binding Proteins PBP2 and PBP3 of Pseudomonas aeruginosa.
Rajavel et al. (2021)
2 more