Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5 (C0RYV6)
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
- C0RYV6
- Type
- protein
- Length
- 689 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Restriction of telomere capping protein 5
- UniProt
- C0RYV6
- Pockets
- 10 · best druggability 0.74
Structure
1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 5 | protein | 689 | 38% helix, 14% strand | C0RYV6 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.74 | 0.96 | 21 | empty |
| 2 | 918 | 0.69 | 0.75 | 87 | empty |
| 3 | 365 | 0.56 | 0.75 | 50 | empty |
| 4 | 99 | 0.50 | 0.82 | 18 | empty |
| 5 | 185 | 0.48 | 0.76 | 31 | 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 C0RYV6
- Elsewhere: UniProt C0RYV6 · AlphaFold DB C0RYV6
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