Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine reductase (Q1I7F9)
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
- Q1I7F9
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- UniProt
- Q1I7F9
- Pockets
- 2 · best druggability 0.57
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 | 276 | 28% helix, 33% strand | Q1I7F9 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.57 | 0.87 | 25 | empty |
| 2 | 107 | 0.43 | 0.78 | 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 Q1I7F9
- Elsewhere: UniProt Q1I7F9 · AlphaFold DB Q1I7F9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.