Research workbench
AlphaFold monomer V2.0 prediction for dtdp-6-deoxy-L-talose 4-dehydrogenase (NAD(P)(+)) (E5F146)
Analyse AlphaFold monomer V2.0 prediction for dtdp-6-deoxy-L-talose 4-dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E5F146
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x943D409fcC503a49f8ABBCEB2544292048F50bD1
- Molecule
- Dtdp-6-deoxy-L-talose 4-dehydrogenase (NAD(P)(+))
- UniProt
- E5F146
- Pockets
- 1 · best druggability 0.77
Structure
1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dtdp-6-deoxy-L-talose 4-dehydrogenase (NAD(P)(+)) | protein | 318 | 39% helix, 19% strand | E5F146 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 847 | 0.77 | 0.80 | 73 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt E5F146
- Elsewhere: UniProt E5F146 · AlphaFold DB E5F146
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.