CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.40 | 3-Layer(aba) Sandwich | 
|   | 3.40.710 | Beta-lactamase | 
|   | 3.40.710.10 | DD-peptidase/beta-lactamase superfamily | 
Domain Context
CATH Clusters
| Superfamily | DD-peptidase/beta-lactamase superfamily | 
| Functional Family | D-alanyl-D-alanine serine-type carboxypeptidase | 
Enzyme Information
| 3.4.16.4 | Serine-type D-Ala-D-Ala carboxypeptidase. based on mapping to UniProt P08506 Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. -!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13. | 
UniProtKB Entries (1)
| P08506 | DACC_ECOLI Escherichia coli K-12 D-alanyl-D-alanine carboxypeptidase DacC | 
PDB Structure
| PDB | 3IT9 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Crystal structures of penicillin-binding protein 6 from Escherichia coli. J.Am.Chem.Soc. | 
