CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.80 | D-tyrosyl-trna(Tyr) Deacylase; Chain: A; |
|
3.50.80.20 | D-Ala-D-Ala carboxypeptidase C, peptidase S13 |
Domain Context
CATH Clusters
| Superfamily | D-Ala-D-Ala carboxypeptidase C, peptidase S13 |
| Functional Family |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P24228
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.
|
| 3.4.21.- |
Serine endopeptidases.
based on mapping to UniProt P24228
|
UniProtKB Entries (1)
| P24228 |
DACB_ECOLI
Escherichia coli K-12
D-alanyl-D-alanine carboxypeptidase DacB
|
PDB Structure
| PDB | 2EX9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics
Biochemistry
|
