MolNFT v1 · #415390 · protein
AlphaFold monomer V2.0 prediction for adenosylcobalamin-dependent ribonucleoside-triphosphate reductase (Q5FMX8)
Q5FMX8: “AlphaFold monomer V2.0 prediction for adenosylcobalamin-dependent ribonucleoside-triphosphate reductase…”. 7 pockets (best druggability 0.82). MolNFT v1 #415390 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5FMX8
- Type
- protein
- Length
- 744 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x59018c174d1Ecad02850b8c56eDC5A53F1C2d4c5
- Molecule
- Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase
- UniProt
- Q5FMX8
- Pockets
- 7 · best druggability 0.82
Structure
1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase | protein | 744 | 40% helix, 17% strand | Q5FMX8 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.82 | 0.83 | 114 | empty |
| 2 | 248 | 0.73 | 0.87 | 31 | empty |
| 3 | 315 | 0.70 | 0.83 | 48 | empty |
| 4 | 209 | 0.48 | 0.75 | 36 | empty |
| 5 | 188 | 0.47 | 0.75 | 21 | 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 Q5FMX8
- Elsewhere: UniProt Q5FMX8 · AlphaFold DB Q5FMX8
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