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AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit (A0RHQ7)
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
- A0RHQ7
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
- UniProt
- A0RHQ7
- Pockets
- 2 · best druggability 0.58
Structure
1 distinct chain · 22% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit | protein | 259 | 22% helix, 37% strand | A0RHQ7 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.58 | 0.79 | 33 | empty |
| 2 | 87 | 0.42 | 0.79 | 18 | 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 A0RHQ7
- Elsewhere: UniProt A0RHQ7 · AlphaFold DB A0RHQ7
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