6g9s

X-ray diffraction
2Å resolution

Structural basis for the inhibition of E. coli PBP2

Released:

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.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan D,D-transpeptidase MrdA Chain: A
Molecule details ›
Chain: A
Length: 582 amino acids
Theoretical weight: 65.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AD65 (Residues: 52-633; Coverage: 92%)
Gene names: JW0630, b0635, mrdA, pbpA
Sequence domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2221
Unit cell:
a: 126.303Å b: 182.806Å c: 75.561Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.216 0.26
Expression system: Escherichia coli BL21