MolNFT v1 · #468914 · protein
AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein 2 (Q5XIK2)
Q5XIK2: “AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein 2 (Q5XIK2)”. 3 pockets (best druggability 0.65). MolNFT v1 #468914 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5XIK2
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc487cEf008e163c9c475e4f157372b0d7968A7cb
- Molecule
- Thioredoxin-related transmembrane protein 2
- UniProt
- Q5XIK2
- Pockets
- 3 · best druggability 0.65
Structure
1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-related transmembrane protein 2 | protein | 295 | 51% helix, 11% strand | Q5XIK2 |
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 | 342 | 0.65 | 0.80 | 52 | empty |
| 2 | 103 | 0.37 | 0.75 | 18 | empty |
| 3 | 55 | 0.30 | 0.74 | 15 | 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 Q5XIK2
- Elsewhere: UniProt Q5XIK2 · AlphaFold DB Q5XIK2
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