Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (A1AVR5)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1AVR5
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7827f7B56a7c719b0EaeD83AF7DF9251AC6C0C19
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- A1AVR5
- Pockets
- 5 · best druggability 0.49
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 417 | 52% helix, 12% strand | A1AVR5 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.49 | 0.86 | 18 | empty |
| 2 | 111 | 0.40 | 0.76 | 16 | empty |
| 3 | 68 | 0.40 | 0.79 | 18 | empty |
| 4 | 101 | 0.36 | 0.74 | 19 | empty |
| 5 | 67 | 0.33 | 0.76 | 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 A1AVR5
- Elsewhere: UniProt A1AVR5 · AlphaFold DB A1AVR5
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