Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (B4E5L5)
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
- B4E5L5
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- B4E5L5
- Pockets
- 3 · best druggability 0.78
Structure
1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 355 | 70% helix, 0% strand | B4E5L5 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.78 | 0.97 | 28 | empty |
| 2 | 276 | 0.59 | 0.78 | 29 | empty |
| 3 | 234 | 0.55 | 0.77 | 28 | 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 B4E5L5
- Elsewhere: UniProt B4E5L5 · AlphaFold DB B4E5L5
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