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 | 5KSH |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Alanine 501 Mutations in Penicillin-Binding Protein 2 from Neisseria gonorrhoeae: Structure, Mechanism, and Effects on Cephalosporin Resistance and Biological Fitness.
Biochemistry
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