Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine reductase (A7MYB6)
Analyse AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7MYB6
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2a931c87A5700ACa8BF19aB91e1bcC88a9EdAebB
- Molecule
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- UniProt
- A7MYB6
- Pockets
- 3 · best druggability 0.55
Structure
1 distinct chain · 28% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent 7-cyano-7-deazaguanine reductase | protein | 281 | 28% helix, 33% strand | A7MYB6 |
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 | 111 | 0.55 | 0.83 | 29 | empty |
| 2 | 82 | 0.47 | 0.82 | 20 | empty |
| 3 | 55 | 0.35 | 0.79 | 12 | 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 A7MYB6
- Elsewhere: UniProt A7MYB6 · AlphaFold DB A7MYB6
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