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:
- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
- Beta-lactamase/transpeptidase-like
- D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily
- Penicillin-binding protein, C-terminal domain superfamily
- Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-140151 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
D-alanyl-D-alanine carboxypeptidase DacC
Molecule details ›
Chains: A, B, C, D
Length: 352 amino acids
Theoretical weight: 38.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 352 amino acids
Theoretical weight: 38.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P08506 (Residues: 28-378; Coverage: 94%)
Sequence domains:
Structure domains:
Ligands and Environments
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
ALS BEAMLINE 8.3.1
Spacegroup:
P21
Expression systems:
- Escherichia coli
- Not provided
