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 |
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
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