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 | Penicillin-binding protein 1B | 
Enzyme Information
| 3.4.16.4 | Serine-type D-Ala-D-Ala carboxypeptidase. based on mapping to UniProt P02919 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. | 
| 2.4.1.129 | Peptidoglycan glycosyltransferase. based on mapping to UniProt P02919 (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)- diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate. -!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. -!- Involved in the synthesis of cell-wall peptidoglycan. | 
UniProtKB Entries (1)
| P02919 | PBPB_ECOLI Escherichia coli K-12 Penicillin-binding protein 1B | 
PDB Structure
| PDB | 5FGZ | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Structural and Kinetic Characterization of Diazabicyclooctanes as Dual Inhibitors of Both Serine-beta-Lactamases and Penicillin-Binding Proteins. Acs Chem.Biol. | 
