Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5 (B6K4Q8)
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
- B6K4Q8
- Type
- protein
- Length
- 493 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Restriction of telomere capping protein 5
- UniProt
- B6K4Q8
- Pockets
- 6 · best druggability 0.73
Structure
1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 5 | protein | 493 | 40% helix, 18% strand | B6K4Q8 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 738 | 0.73 | 0.79 | 66 | empty |
| 2 | 329 | 0.62 | 0.79 | 40 | empty |
| 3 | 194 | 0.58 | 0.81 | 25 | empty |
| 4 | 55 | 0.50 | 0.87 | 20 | empty |
| 5 | 86 | 0.35 | 0.75 | 20 | 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 B6K4Q8
- Elsewhere: UniProt B6K4Q8 · AlphaFold DB B6K4Q8
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