Research workbench
AlphaFold monomer V2.0 prediction for thrombospondin type-1 domain- containing protein 1 (Q5BIR3)
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
- Q5BIR3
- Type
- protein
- Length
- 849 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3Fb036B69Ae373B7B8D5715E6f811A5c94260042
- Molecule
- Thrombospondin type-1 domain-containing protein 1
- UniProt
- Q5BIR3
- Pockets
- 4 · best druggability 0.58
Structure
1 distinct chain · 9% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thrombospondin type-1 domain-containing protein 1 | protein | 849 | 9% helix, 21% strand | Q5BIR3 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.58 | 0.81 | 25 | empty |
| 2 | 115 | 0.53 | 0.83 | 23 | empty |
| 3 | 57 | 0.29 | 0.74 | 15 | empty |
| 4 | 55 | 0.25 | 0.73 | 15 | 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 Q5BIR3
- Elsewhere: UniProt Q5BIR3 · AlphaFold DB Q5BIR3
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