Research workbench
Crystal structure of human thioredoxin C69/73S double-mutant, oxidized form
Analyse Crystal structure of human thioredoxin C69/73S double-mutant, oxidized form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M9K
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.5
- Source
- Homo sapiens
- Molecule
- Thioredoxin
- UniProt
- P10599
- Ligands
- D1D, SO4
- Pockets
- 2 · best druggability 0.32
Structure
x-ray diffraction · resolution 1.5 · 1 distinct chain · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thioredoxin | protein | 105 | 41% helix, 27% strand | P10599 |
Ligands and binding sites
- D1D · (4S,5S)-1,2-dithiane-4,5-diol · ligand · chains B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.32 | 0.75 | 15 | D1D |
| 2 | 52 | 0.31 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 328 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 3M9K · PDBe 3M9K · UniProt P10599
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