Research workbench
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit F (A1KSH3)
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
- A1KSH3
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661E995327D4c9b99E17Cca11ea8072ed8a218Dd
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit F
- UniProt
- A1KSH3
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit F | protein | 405 | 33% helix, 28% strand | A1KSH3 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 628 | 0.71 | 0.79 | 59 | empty |
| 2 | 124 | 0.42 | 0.76 | 22 | empty |
| 3 | 75 | 0.33 | 0.75 | 16 | empty |
| 4 | 56 | 0.29 | 0.75 | 17 | 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 A1KSH3
- Elsewhere: UniProt A1KSH3 · AlphaFold DB A1KSH3
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