Research workbench
The crystal structure of the K18G mutant of the thioredoxin from alicyclobacillus acidocaldarius
Analyse The crystal structure of the K18G mutant of the thioredoxin from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NSW
- Type
- protein
- Length
- 420 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin
- EC
- 1.8.1.9
- UniProt
- P80579
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Thioredoxin (EC 1.8.1.9) | protein | 105 | 32% helix, 27% strand | P80579 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 698 | 0.73 | 0.79 | 40 | empty |
| 2 | 143 | 0.41 | 0.74 | 27 | empty |
| 3 | 70 | 0.33 | 0.75 | 19 | empty |
Interfaces
5 interfaces between chains.
- A–B · 606 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 592 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 503 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 185 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 180 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1NSW · The Crystal Structure of the K18G Mutant of the thioredoxin from Alicyclobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- P80579 · AlphaFold monomer V2.0 prediction for thioredoxin (P80579) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P80579
- Elsewhere: RCSB PDB 1NSW · PDBe 1NSW · UniProt P80579
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