Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 1 (B9WN49)
Analyse AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9WN49
- Type
- protein
- Length
- 1,098 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa53776A41fB2e67da75A96E8a53746b6874aAB4
- Molecule
- Restriction of telomere capping protein 1
- UniProt
- B9WN49
- Pockets
- 8 · best druggability 0.79
Structure
1 distinct chain · 16% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 1 | protein | 1098 | 16% helix, 17% strand | B9WN49 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 913 | 0.79 | 0.81 | 73 | empty |
| 2 | 413 | 0.66 | 0.79 | 42 | empty |
| 3 | 411 | 0.62 | 0.76 | 43 | empty |
| 4 | 183 | 0.57 | 0.80 | 27 | empty |
| 5 | 222 | 0.52 | 0.76 | 27 | 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 B9WN49
- Elsewhere: UniProt B9WN49 · AlphaFold DB B9WN49
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