Research workbench
AlphaFold monomer V2.0 prediction for adenosylhomocysteinase (Q8KEG8)
Analyse AlphaFold monomer V2.0 prediction for adenosylhomocysteinase (Q8KEG8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8KEG8
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Adenosylhomocysteinase
- UniProt
- Q8KEG8
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosylhomocysteinase | protein | 471 | 46% helix, 15% strand | Q8KEG8 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 428 | 0.74 | 0.84 | 75 | empty |
| 2 | 317 | 0.55 | 0.75 | 45 | empty |
| 3 | 186 | 0.50 | 0.77 | 25 | empty |
| 4 | 111 | 0.40 | 0.76 | 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 Q8KEG8
- Elsewhere: UniProt Q8KEG8 · AlphaFold DB Q8KEG8
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