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AlphaFold monomer V2.0 prediction for torsin-1A-interacting protein 2, isoform IFRG15 (Q9H496)
Analyse AlphaFold monomer V2.0 prediction for torsin-1A-interacting protein 2, isoform… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9H496
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Torsin-1A-interacting protein 2, isoform IFRG15
- UniProt
- Q9H496
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 59% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Torsin-1A-interacting protein 2, isoform IFRG15 | protein | 131 | 59% helix, 2% strand | Q9H496 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.56 | 0.78 | 24 | empty |
| 2 | 77 | 0.42 | 0.79 | 14 | empty |
| 3 | 71 | 0.34 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 1 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 Q9H496
- Elsewhere: UniProt Q9H496 · AlphaFold DB Q9H496
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