Research workbench
AlphaFold monomer V2.0 prediction for testis anion transporter 1 (Q96RN1)
Analyse AlphaFold monomer V2.0 prediction for testis anion transporter 1 (Q96RN1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96RN1
- Type
- protein
- Length
- 970 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- Testis anion transporter 1
- UniProt
- Q96RN1
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 43% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Testis anion transporter 1 | protein | 970 | 43% helix, 6% strand | Q96RN1 |
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 | 308 | 0.72 | 0.85 | 47 | empty |
| 2 | 271 | 0.59 | 0.79 | 42 | empty |
| 3 | 106 | 0.36 | 0.74 | 15 | empty |
| 4 | 70 | 0.33 | 0.76 | 15 | empty |
| 5 | 64 | 0.33 | 0.76 | 16 | empty |
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 Q96RN1
- Elsewhere: UniProt Q96RN1 · AlphaFold DB Q96RN1
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