Research workbench
AlphaFold monomer V2.0 prediction for anaerobic ribonucleoside- triphosphate reductase (Q9L646)
Analyse AlphaFold monomer V2.0 prediction for anaerobic ribonucleoside- triphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9L646
- Type
- protein
- Length
- 712 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7BeA38dAb4565F0858708331148660F2A14d4201
- Molecule
- Anaerobic ribonucleoside-triphosphate reductase
- UniProt
- Q9L646
- Pockets
- 8 · best druggability 0.81
Structure
1 distinct chain · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anaerobic ribonucleoside-triphosphate reductase | protein | 712 | 49% helix, 13% strand | Q9L646 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.81 | 0.87 | 56 | empty |
| 2 | 80 | 0.74 | 0.97 | 24 | empty |
| 3 | 291 | 0.61 | 0.79 | 23 | empty |
| 4 | 192 | 0.50 | 0.77 | 27 | empty |
| 5 | 61 | 0.48 | 0.85 | 19 | 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 Q9L646
- Elsewhere: UniProt Q9L646 · AlphaFold DB Q9L646
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