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AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit (Q97R66)
Analyse AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase B (NAD(+))… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q97R66
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC17d31fe90ba2F028F3A7B668B9af47b13aB2683
- Molecule
- Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
- UniProt
- Q97R66
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 19% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit | protein | 250 | 19% helix, 34% strand | Q97R66 |
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 | 269 | 0.66 | 0.82 | 27 | empty |
| 2 | 131 | 0.42 | 0.76 | 29 | empty |
| 3 | 55 | 0.27 | 0.73 | 19 | 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 Q97R66
- Elsewhere: UniProt Q97R66 · AlphaFold DB Q97R66
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