Research workbench
AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase a (fumarate) (Q53ZE5)
Analyse AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase a (fumarate)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q53ZE5
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Dihydroorotate dehydrogenase a (fumarate)
- UniProt
- Q53ZE5
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroorotate dehydrogenase a (fumarate) | protein | 311 | 37% helix, 19% strand | Q53ZE5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.76 | 0.90 | 50 | empty |
| 2 | 107 | 0.55 | 0.84 | 21 | empty |
| 3 | 64 | 0.31 | 0.75 | 17 | 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 Q53ZE5
- Elsewhere: UniProt Q53ZE5 · AlphaFold DB Q53ZE5
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