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Crystal structure of oxidized ACHT1
Analyse Crystal structure of oxidized ACHT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LYX
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.696
- Source
- Arabidopsis thaliana
- Molecule
- Thioredoxin-like 2-1, chloroplastic
- UniProt
- Q8LEK4
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · resolution 1.696 · 2 distinct chains · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-like 2-1, chloroplastic | protein | 117 | 42% helix, 26% strand | Q8LEK4 |
| B | Thioredoxin-like 2-1, chloroplastic | protein | 122 | 42% helix, 25% strand | Q8LEK4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.41 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 503 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 Q8LEK4
- Elsewhere: RCSB PDB 6LYX · PDBe 6LYX · UniProt Q8LEK4
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