CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1310 | Penicillin-binding protein 2a (Domain 2) |
|
3.90.1310.10 | Penicillin-binding protein 2a (Domain 2) |
Domain Context
CATH Clusters
| Superfamily | Penicillin-binding protein 2a (Domain 2) |
| Functional Family |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P08149
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)
| P08149 |
PBP2_NEIGO
Neisseria gonorrhoeae
Probable peptidoglycan D,D-transpeptidase PenA
|
PDB Structure
| PDB | 3EQV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structures of Penicillin-binding Protein 2 from Penicillin-susceptible and -resistant Strains of Neisseria gonorrhoeae Reveal an Unexpectedly Subtle Mechanism for Antibiotic Resistance.
J.Biol.Chem.
|
