Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (B7GME7)
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
- B7GME7
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8BC40077C5d5F33D23534b61A4486FB35E477897
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- B7GME7
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 333 | 70% helix, 0% strand | B7GME7 |
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 | 268 | 0.60 | 0.79 | 29 | empty |
| 2 | 88 | 0.36 | 0.74 | 15 | empty |
| 3 | 56 | 0.30 | 0.74 | 13 | 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 B7GME7
- Elsewhere: UniProt B7GME7 · AlphaFold DB B7GME7
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