Research workbench
Computationally designed thioredoxin subjected to stability optimizing mutations.
Analyse Computationally designed thioredoxin subjected to stability optimizing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q3K
- Type
- protein
- Length
- 312 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.25
- Source
- synthetic construct
- Molecule
- eMM9
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · resolution 2.25 · 1 distinct chain · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | eMM9 | protein | 104 | 40% helix, 27% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 904 | 0.71 | 0.76 | 64 | empty |
| 2 | 59 | 0.29 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 367 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 133 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 88 Ų buried · 3 hydrogen bonds · protein-protein
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7Q3K · PDBe 7Q3K
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