Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5 (C5MCY0)
Analyse AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5MCY0
- Type
- protein
- Length
- 625 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf0CDB940dff0d2A4aE64023A82962025320FAF68
- Molecule
- Restriction of telomere capping protein 5
- UniProt
- C5MCY0
- Pockets
- 8 · best druggability 0.59
Structure
1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 5 | protein | 625 | 38% helix, 17% strand | C5MCY0 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.59 | 0.92 | 15 | empty |
| 2 | 307 | 0.58 | 0.77 | 41 | empty |
| 3 | 130 | 0.45 | 0.77 | 18 | empty |
| 4 | 116 | 0.44 | 0.78 | 21 | empty |
| 5 | 58 | 0.38 | 0.79 | 13 | 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 C5MCY0
- Elsewhere: UniProt C5MCY0 · AlphaFold DB C5MCY0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.