1hvb

X-ray diffraction
1.17Å resolution

CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN

Released:
Source organism: Streptomyces sp. R61
Primary publication:
A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis.
Proc Natl Acad Sci U S A 98 1427-31 (2001)
PMID: 11171967

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)
PDBe Complex ID:
PDB-CPX-147403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl-D-alanine carboxypeptidase Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 37.42 KDa
Source organism: Streptomyces sp. R61
UniProt:
  • Canonical: P15555 (Residues: 32-380; Coverage: 93%)
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 50.778Å b: 66.664Å c: 100.928Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.114 0.113 0.153