Research workbench
AlphaFold monomer V2.0 prediction for adenosylhomocysteinase (Q5JED2)
Analyse AlphaFold monomer V2.0 prediction for adenosylhomocysteinase (Q5JED2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5JED2
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x727D03690E0ac68C9a3242921fC850514E2AA0C1
- Molecule
- Adenosylhomocysteinase
- UniProt
- Q5JED2
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosylhomocysteinase | protein | 421 | 48% helix, 18% strand | Q5JED2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.72 | 0.85 | 52 | empty |
| 2 | 96 | 0.39 | 0.76 | 17 | empty |
| 3 | 51 | 0.25 | 0.72 | 13 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q5JED2
- Elsewhere: UniProt Q5JED2 · AlphaFold DB Q5JED2
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