1esi

X-ray diffraction
1.8Å resolution

R248L MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

Released:
Source organism: Streptomyces sp. K15
Primary publication:
DD-TRANSPEPTIDASE
To be published

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl-D-alanine carboxypeptidase Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 27.46 KDa
Source organism: Streptomyces sp. K15
Expression system: Streptomyces lividans TK24
UniProt:
  • Canonical: P39042 (Residues: 30-291; Coverage: 100%)
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE D41A
Spacegroup: P212121
Unit cell:
a: 51.01Å b: 51.75Å c: 84.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.233
Expression system: Streptomyces lividans TK24