Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5 (B6H464)
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
- B6H464
- Type
- protein
- Length
- 642 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbF8467B100eddcD57b40BcA629dAe7126b34CBf1
- Molecule
- Restriction of telomere capping protein 5
- UniProt
- B6H464
- Pockets
- 10 · best druggability 0.60
Structure
1 distinct chain · 34% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 5 | protein | 642 | 34% helix, 14% strand | B6H464 |
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 | 218 | 0.60 | 0.81 | 36 | empty |
| 2 | 349 | 0.58 | 0.76 | 52 | empty |
| 3 | 236 | 0.56 | 0.78 | 34 | empty |
| 4 | 186 | 0.56 | 0.80 | 39 | empty |
| 5 | 147 | 0.45 | 0.76 | 16 | 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 B6H464
- Elsewhere: UniProt B6H464 · AlphaFold DB B6H464
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