Research workbench
AlphaFold monomer V2.0 prediction for tetratricopeptide repeat protein 17 (Q96AE7)
Analyse AlphaFold monomer V2.0 prediction for tetratricopeptide repeat protein 17… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96AE7
- Type
- protein
- Length
- 1,141 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80c65687F966a6264124948aC6721671E4B4d776
- Molecule
- Tetratricopeptide repeat protein 17
- UniProt
- Q96AE7
- Pockets
- 17 · best druggability 0.66
Structure
1 distinct chain · 52% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetratricopeptide repeat protein 17 | protein | 1141 | 52% helix, 1% strand | Q96AE7 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 413 | 0.66 | 0.79 | 35 | empty |
| 2 | 554 | 0.63 | 0.75 | 60 | empty |
| 3 | 260 | 0.58 | 0.78 | 32 | empty |
| 4 | 372 | 0.57 | 0.75 | 41 | empty |
| 5 | 191 | 0.54 | 0.79 | 28 | empty |
Modifications
Observed in the structure: 8 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 Q96AE7
- Elsewhere: UniProt Q96AE7 · AlphaFold DB Q96AE7
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