Research workbench
AlphaFold monomer V2.0 prediction for transforming growth factor beta-1 proprotein (O93449)
Analyse AlphaFold monomer V2.0 prediction for transforming growth factor beta-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O93449
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x882B14FbCEd9AA8538F421f0Fc2Be75789f3B8A0
- Molecule
- Transforming growth factor beta-1 proprotein
- UniProt
- O93449
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor beta-1 proprotein | protein | 382 | 26% helix, 29% strand | O93449 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.61 | 0.77 | 31 | empty |
| 2 | 225 | 0.57 | 0.79 | 27 | empty |
| 3 | 52 | 0.52 | 0.88 | 13 | empty |
| 4 | 129 | 0.35 | 0.72 | 21 | empty |
Modifications
Observed in the structure: 4 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 O93449
- Elsewhere: UniProt O93449 · AlphaFold DB O93449
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