MolNFT v1 · #16237 · protein
The crystal structure of the K18G mutant of the thioredoxin from alicyclobacillus acidocaldarius
1NSW: “The crystal structure of the K18G mutant of the thioredoxin from alicyclobacillus acidocaldarius”. X-ray diffraction, 3 pockets (best druggability 0.73). MolNFT v1 #16237 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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