Research workbench
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit E (B5FBI4)
Analyse AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5FBI4
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x58c88c52e15365f7174D3f46cA5b685a9Cb994Db
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit E
- UniProt
- B5FBI4
- Pockets
- 1 · best druggability 0.32
Structure
1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit E | protein | 198 | 78% helix, 0% strand | B5FBI4 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.32 | 0.76 | 12 | 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 B5FBI4
- Elsewhere: UniProt B5FBI4 · AlphaFold DB B5FBI4
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