UniProt Q3Y185
L,D-transpeptidase (Q3Y185)
L,D-transpeptidase (UniProt Q3Y185), EC 2.3.2.12: 8 experimental structures on GenesisL1, 3 ligands bound, 16 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q3Y185
- Protein
- L,D-transpeptidase
- EC
- 2.3.2.12
- Experimental structures
- 8
- Predicted models
- 0
- Ligands
- 3
- Pockets
- 16 · 2 records with a druggable one
Structures
8 records of Q3Y185 in the MolNFT archive: 8 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1ZAT | Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution | x-ray diffraction | A | ZN, SO4 | 2 (best 0.36) |
| 1ZAT | Crystal structure of an enterococcus faecium peptidoglycan binding protein at 2.4 a resolution | x-ray diffraction | A | ZN, SO4 | 2 (best 0.36) |
| 2HKL | Crystal structure of Enterococcus faecium L,D-transpeptidase C442S mutant | x-ray diffraction | A, B, C | SO4 | 5 (best 0.71) |
| 2HKL | Crystal structure of enterococcus faecium L,D-transpeptidase C442S mutant | x-ray diffraction | A, B, C | SO4 | 5 (best 0.71) |
| 3ZG4 | NMR structure of the catalytic domain from E. faecium L,D- transpeptidase | solution nmr | A | — | — |
| 3ZG4 | NMR structure of the catalytic domain from E. faecium L,D- transpeptidase | solution nmr | A | — | — |
| 3ZGP | NMR structure of the catalytic domain from E. faecium L,D- transpeptidase acylated by ertapenem | solution nmr | A | 1RG | 1 (best 0.38) |
| 3ZGP | NMR structure of the catalytic domain from E. faecium L,D- transpeptidase acylated by ertapenem | solution nmr | A | 1RG | 1 (best 0.38) |
Ligands
Elsewhere
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