Research workbench
AlphaFold monomer V2.0 prediction for thrombospondin type-1 domain- containing protein 1 (Q9NS62)
Analyse AlphaFold monomer V2.0 prediction for thrombospondin type-1 domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9NS62
- Type
- protein
- Length
- 852 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Thrombospondin type-1 domain-containing protein 1
- UniProt
- Q9NS62
- Pockets
- 3 · best druggability 0.46
Structure
1 distinct chain · 10% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thrombospondin type-1 domain-containing protein 1 | protein | 852 | 10% helix, 21% strand | Q9NS62 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.46 | 0.82 | 22 | empty |
| 2 | 106 | 0.45 | 0.79 | 18 | empty |
| 3 | 102 | 0.37 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
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 Q9NS62
- Elsewhere: UniProt Q9NS62 · AlphaFold DB Q9NS62
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