Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine reductase (Q2G586)
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
- Q2G586
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- UniProt
- Q2G586
- Pockets
- 2 · best druggability 0.51
Structure
1 distinct chain · 17% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent 7-cyano-7-deazaguanine reductase | protein | 166 | 17% helix, 27% strand | Q2G586 |
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 | 156 | 0.51 | 0.79 | 27 | empty |
| 2 | 60 | 0.31 | 0.75 | 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 Q2G586
- Elsewhere: UniProt Q2G586 · AlphaFold DB Q2G586
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