Research workbench
AlphaFold monomer V2.0 prediction for oxidoreductase NAD-binding domain-containing protein 1 (Q96HP4)
Analyse AlphaFold monomer V2.0 prediction for oxidoreductase NAD-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96HP4
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd393e9C88bA5c6DEea9896608891D41961116AB6
- Molecule
- Oxidoreductase NAD-binding domain-containing protein 1
- UniProt
- Q96HP4
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 24% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase NAD-binding domain-containing protein 1 | protein | 312 | 24% helix, 26% strand | Q96HP4 |
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 | 316 | 0.65 | 0.80 | 41 | empty |
| 2 | 71 | 0.38 | 0.77 | 13 | empty |
| 3 | 71 | 0.30 | 0.74 | 18 | empty |
| 4 | 54 | 0.28 | 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 Q96HP4
- Elsewhere: UniProt Q96HP4 · AlphaFold DB Q96HP4
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