Research workbench
Crystal structure of lactococcus lactis thioredoxin reductase (fo conformation)
Analyse Crystal structure of lactococcus lactis thioredoxin reductase (fo conformation) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MJK
- Type
- protein
- Length
- 1,208 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase
- EC
- 1.8.1.9
- UniProt
- A0A166TWQ7
- Ligands
- FAD, SO4
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Thioredoxin reductase (EC 1.8.1.9) | protein | 302 | 26% helix, 31% strand | A0A166TWQ7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 655 | 0.82 | 0.87 | 89 | FAD, SO4 |
| 2 | 611 | 0.81 | 0.86 | 74 | FAD |
| 3 | 1020 | 0.81 | 0.82 | 99 | FAD, SO4 |
| 4 | 963 | 0.80 | 0.82 | 98 | FAD, SO4 |
| 5 | 469 | 0.78 | 0.86 | 61 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2124 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 2112 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 895 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5MJK · Crystal Structure of Lactococcus lactis Thioredoxin Reductase (FO conformation) · 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 A0A166TWQ7
- Elsewhere: RCSB PDB 5MJK · PDBe 5MJK · UniProt A0A166TWQ7
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