Research workbench
The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
Analyse The high-resolution three-dimensional solution structures of the oxidized and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TRU
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin
- UniProt
- P10599
Structure
solution nmr · 1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin | protein | 105 | 30% helix, 28% strand | P10599 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1TRU · The high-resolution three-dimensional solution structures of the oxidized and reduced… · the same entry in another collection · chain A against A, TM-score 1.00
- P10599 · AlphaFold monomer V2.0 prediction for thioredoxin (P10599) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P10599
- Elsewhere: RCSB PDB 1TRU · PDBe 1TRU · UniProt P10599
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