Research workbench
AlphaFold monomer V2.0 prediction for transforming growth factor beta-2 proprotein (P27090)
Analyse AlphaFold monomer V2.0 prediction for transforming growth factor beta-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27090
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Transforming growth factor beta-2 proprotein
- UniProt
- P27090
- Pockets
- 6 · best druggability 0.60
Structure
1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor beta-2 proprotein | protein | 414 | 29% helix, 27% strand | P27090 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.60 | 0.74 | 43 | empty |
| 2 | 131 | 0.42 | 0.75 | 18 | empty |
| 3 | 130 | 0.40 | 0.74 | 22 | empty |
| 4 | 80 | 0.33 | 0.74 | 12 | empty |
| 5 | 56 | 0.31 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 5TX6 · Structure of TGF-BETA2 derivative with deletion of residues 52-71 and 10 single amino… · an experimental structure of the same protein · chain A against B, TM-score 0.20
- 5TX6 · Structure of TGF-beta2 derivative with deletion of residues 52-71 and 10 single amino… · an experimental structure of the same protein · chain A against B, TM-score 0.20
- 5TX2 · Miniature TGF-beta2 3-mutant monomer · an experimental structure of the same protein · chain A against B, TM-score 0.20
- 5TX2 · Miniature TGF-BETA2 3-mutant monomer · an experimental structure of the same protein · chain A against A, TM-score 0.20
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 P27090
- Elsewhere: UniProt P27090 · AlphaFold DB P27090
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