Research workbench
AlphaFold monomer V2.0 prediction for oxygen-dependent choline dehydrogenase (B2TCJ8)
Analyse AlphaFold monomer V2.0 prediction for oxygen-dependent choline dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2TCJ8
- Type
- protein
- Length
- 561 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Oxygen-dependent choline dehydrogenase
- UniProt
- B2TCJ8
- Pockets
- 3 · best druggability 0.86
Structure
1 distinct chain · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxygen-dependent choline dehydrogenase | protein | 561 | 27% helix, 24% strand | B2TCJ8 |
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 | 340 | 0.86 | 0.96 | 58 | empty |
| 2 | 230 | 0.71 | 0.87 | 33 | empty |
| 3 | 57 | 0.30 | 0.76 | 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 B2TCJ8
- Elsewhere: UniProt B2TCJ8 · AlphaFold DB B2TCJ8
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