› 1es5

X-ray diffraction
1.4Å resolution

S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

Released:
DOI: 10.2210/pdb1es5/pdb
PDB entry 1es5 coloured by chain, front view.
PDB entry 1es5 coloured by chain, side view.
PDB entry 1es5 coloured by chain, top view.
Source organism: Streptomyces sp. K15
Entry authors: Fonze E, Charlier P

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153808 (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: 27.49 KDa
Source organism: Streptomyces sp. K15
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39042 (Residues: 30-291; Coverage: 100%)
Sequence domains: D-alanyl-D-alanine carboxypeptidase
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 DW32
Spacegroup: P212121
Unit cell:
a: 45.93Å b: 53.756Å c: 105.061Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.245
Expression system: Escherichia coli BL21(DE3)

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