Research workbench
AlphaFold monomer V2.0 prediction for vitamin B12-dependent ribonucleotide reductase (O54196)
Analyse AlphaFold monomer V2.0 prediction for vitamin B12-dependent ribonucleotide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O54196
- Type
- protein
- Length
- 961 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Vitamin B12-dependent ribonucleotide reductase
- UniProt
- O54196
- Pockets
- 8 · best druggability 0.81
Structure
1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin B12-dependent ribonucleotide reductase | protein | 961 | 40% helix, 16% strand | O54196 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 842 | 0.81 | 0.84 | 103 | empty |
| 2 | 150 | 0.54 | 0.81 | 36 | empty |
| 3 | 128 | 0.52 | 0.81 | 25 | empty |
| 4 | 86 | 0.49 | 0.82 | 18 | empty |
| 5 | 63 | 0.35 | 0.78 | 22 | empty |
Modifications
Observed in the structure: 3 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 O54196
- Elsewhere: UniProt O54196 · AlphaFold DB O54196
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