Research workbench
AlphaFold monomer V2.0 prediction for 7-cyano-7-deazaguanine synthase (A1VX95)
Analyse AlphaFold monomer V2.0 prediction for 7-cyano-7-deazaguanine synthase (A1VX95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1VX95
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x09c4b87fe92D650202Fe96778872a3ffe97fE80C
- Molecule
- 7-cyano-7-deazaguanine synthase
- UniProt
- A1VX95
- Pockets
- 1 · best druggability 0.82
Structure
1 distinct chain · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 7-cyano-7-deazaguanine synthase | protein | 224 | 40% helix, 13% strand | A1VX95 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.82 | 0.90 | 55 | 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 A1VX95
- Elsewhere: UniProt A1VX95 · AlphaFold DB A1VX95
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