Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine reductase (A8GQN6)
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
- A8GQN6
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- UniProt
- A8GQN6
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent 7-cyano-7-deazaguanine reductase | protein | 273 | 26% helix, 34% strand | A8GQN6 |
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 | 129 | 0.69 | 0.90 | 25 | empty |
| 2 | 124 | 0.50 | 0.80 | 22 | 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 A8GQN6
- Elsewhere: UniProt A8GQN6 · AlphaFold DB A8GQN6
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