MolNFT v1 · #268941 · protein
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit F (A6VLY1)
A6VLY1 · Na(+)-translocating NADH-quinone reductase subunit F: “AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit F (A6VLY1)”. 3 pockets (best druggability 0.71). MolNFT v1 #268941 on GenesisL1: 3D…
- Accession
- A6VLY1
- Type
- protein
- Length
- 409 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit F
- UniProt
- A6VLY1
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit F | protein | 409 | 32% helix, 29% strand | A6VLY1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.71 | 0.78 | 65 | empty |
| 2 | 136 | 0.46 | 0.77 | 27 | empty |
| 3 | 97 | 0.41 | 0.78 | 21 | 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 A6VLY1
- Elsewhere: UniProt A6VLY1 · AlphaFold DB A6VLY1
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