Research workbench
AlphaFold monomer V2.0 prediction for transforming growth factor beta-3 proprotein (P17125)
Analyse AlphaFold monomer V2.0 prediction for transforming growth factor beta-3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P17125
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Transforming growth factor beta-3 proprotein
- UniProt
- P17125
- Pockets
- 5 · best druggability 0.71
Structure
1 distinct chain · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor beta-3 proprotein | protein | 410 | 26% helix, 26% strand | P17125 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 837 | 0.71 | 0.77 | 73 | empty |
| 2 | 399 | 0.62 | 0.77 | 38 | empty |
| 3 | 114 | 0.44 | 0.77 | 15 | empty |
| 4 | 51 | 0.29 | 0.76 | 12 | empty |
| 5 | 58 | 0.28 | 0.73 | 15 | 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 P17125
- Elsewhere: UniProt P17125 · AlphaFold DB P17125
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