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AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit (A0AJT9)
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
- A0AJT9
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8B97cB2b61CB3E56705D4C4e7d1809E1aE1BDC69
- Molecule
- Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
- UniProt
- A0AJT9
- Pockets
- 2 · best druggability 0.63
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 | 254 | 22% helix, 37% strand | A0AJT9 |
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 | 287 | 0.63 | 0.80 | 35 | empty |
| 2 | 105 | 0.39 | 0.76 | 22 | 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 A0AJT9
- Elsewhere: UniProt A0AJT9 · AlphaFold DB A0AJT9
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