Research workbench
AlphaFold monomer V2.0 prediction for vitamin B12-dependent ribonucleotide reductase (Q72S00)
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
- Q72S00
- Type
- protein
- Length
- 1,201 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa640C227040600dbC67F66f02Af7651c7D2D9822
- Molecule
- Vitamin B12-dependent ribonucleotide reductase
- UniProt
- Q72S00
- Pockets
- 11 · best druggability 0.81
Structure
1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin B12-dependent ribonucleotide reductase | protein | 1201 | 40% helix, 14% strand | Q72S00 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1173 | 0.81 | 0.82 | 110 | empty |
| 2 | 572 | 0.68 | 0.77 | 53 | empty |
| 3 | 309 | 0.64 | 0.80 | 31 | empty |
| 4 | 432 | 0.60 | 0.75 | 53 | empty |
| 5 | 117 | 0.55 | 0.83 | 21 | empty |
Modifications
Observed in the structure: 2 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 Q72S00
- Elsewhere: UniProt Q72S00 · AlphaFold DB Q72S00
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.