Research workbench
Crystal structure of a thioredoxin from Clostridium acetobutylicum at 1.75 A resolution
Analyse Crystal structure of a thioredoxin from Clostridium acetobutylicum at 1.75 A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GN9
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Clostridium acetobutylicum ATCC 824
- Molecule
- Thioredoxin
- UniProt
- Q97EM7
Structure
x-ray diffraction · resolution 1.75 · 1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin | protein | 102 | 39% helix, 26% strand | Q97EM7 |
Ligands and binding sites
- ACT · Acetate ion · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GN9 · Crystal structure of a thioredoxin from clostridium acetobutylicum at 1.75 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
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 Q97EM7
- Elsewhere: RCSB PDB 6GN9 · PDBe 6GN9 · UniProt Q97EM7
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