Research workbench
AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein 1 (Q9H3N1)
Analyse AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9H3N1
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6239Ad87AbE06b781175d476DB7715eEa7E05E2f
- Molecule
- Thioredoxin-related transmembrane protein 1
- UniProt
- Q9H3N1
Structure
1 distinct chain · 38% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-related transmembrane protein 1 | protein | 280 | 38% helix, 9% strand | Q9H3N1 |
Compared structures
- 1X5E · The solution structure of the thioredoxin-like domain of human thioredoxin-related… · an experimental structure of the same protein · chain A against A, TM-score 0.41
- 1X5E · The solution structure of the thioredoxin-like domain of human Thioredoxin-related… · an experimental structure of the same protein · chain A against A, TM-score 0.41
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 Q9H3N1
- Elsewhere: UniProt Q9H3N1 · AlphaFold DB Q9H3N1
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