Research workbench
AlphaFold monomer V2.0 prediction for transforming growth factor beta-1 proprotein (P16176)
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
- P16176
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x00c8B315905B14eEc67079b1ceA660779D5A86C1
- Molecule
- Transforming growth factor beta-1 proprotein
- UniProt
- P16176
- Pockets
- 6 · best druggability 0.64
Structure
1 distinct chain · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor beta-1 proprotein | protein | 382 | 28% helix, 32% strand | P16176 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.64 | 0.82 | 33 | empty |
| 2 | 279 | 0.64 | 0.81 | 39 | empty |
| 3 | 100 | 0.45 | 0.79 | 22 | empty |
| 4 | 105 | 0.41 | 0.76 | 17 | empty |
| 5 | 104 | 0.37 | 0.74 | 18 | 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 P16176
- Elsewhere: UniProt P16176 · AlphaFold DB P16176
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