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AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit (C1KWD3)
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
- C1KWD3
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7beC3Ef9c210E66D52B594848B0A7dB52F1cD5c4
- Molecule
- Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
- UniProt
- C1KWD3
- Pockets
- 2 · best druggability 0.63
Structure
1 distinct chain · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit | protein | 254 | 19% helix, 37% strand | C1KWD3 |
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 | 227 | 0.63 | 0.82 | 22 | empty |
| 2 | 92 | 0.42 | 0.78 | 24 | 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 C1KWD3
- Elsewhere: UniProt C1KWD3 · AlphaFold DB C1KWD3
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