Research workbench
AlphaFold monomer V2.0 prediction for tripartite motif-containing protein 29 (Q8R2Q0)
Analyse AlphaFold monomer V2.0 prediction for tripartite motif-containing protein 29… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8R2Q0
- Type
- protein
- Length
- 587 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x42dD77B72587842B0D45dDAfeE209818D57836d0
- Molecule
- Tripartite motif-containing protein 29
- UniProt
- Q8R2Q0
- Pockets
- 4 · best druggability 0.43
Structure
1 distinct chain · 29% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripartite motif-containing protein 29 | protein | 587 | 29% helix, 4% strand | Q8R2Q0 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.43 | 0.74 | 27 | empty |
| 2 | 108 | 0.38 | 0.74 | 17 | empty |
| 3 | 120 | 0.37 | 0.73 | 21 | empty |
| 4 | 72 | 0.29 | 0.73 | 18 | empty |
Compared structures
- 8SDE · Electrostatic-Mediated Tetramerization of the Coiled-Coil Domain in TRIM29 · an experimental structure of the same protein · chain A against A, TM-score 0.14
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 Q8R2Q0
- Elsewhere: UniProt Q8R2Q0 · AlphaFold DB Q8R2Q0
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