Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (P0AFD5)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AFD5
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- P0AFD5
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 325 | 72% helix, 1% strand | P0AFD5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.61 | 0.80 | 38 | empty |
| 2 | 118 | 0.52 | 0.80 | 20 | empty |
| 3 | 118 | 0.42 | 0.75 | 18 | 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 P0AFD5
- Elsewhere: UniProt P0AFD5 · AlphaFold DB P0AFD5
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