Research workbench
Crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with reduced C-terminal tail
Analyse Crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EAN
- Type
- protein
- Length
- 2,936 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase 1
- EC
- 1.8.1.9
- UniProt
- O89049
- Ligands
- FAD, NAP
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Thioredoxin reductase 1 (EC 1.8.1.9) | protein | 490 | 33% helix, 26% strand | O89049 |
| C | Thioredoxin reductase 1 (EC 1.8.1.9) | protein | 486 | 34% helix, 26% strand | O89049 |
| D | Thioredoxin reductase 1 (EC 1.8.1.9) | protein | 491 | 32% helix, 26% strand | O89049 |
| F | Thioredoxin reductase 1 (EC 1.8.1.9) | protein | 489 | 33% helix, 26% strand | O89049 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 6 copies · chains A, B, C, D, E, F
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1104 | 0.87 | 0.88 | 115 | empty |
| 2 | 602 | 0.86 | 0.91 | 70 | empty |
| 3 | 798 | 0.85 | 0.88 | 92 | empty |
| 4 | 764 | 0.85 | 0.88 | 83 | empty |
| 5 | 966 | 0.82 | 0.83 | 113 | FAD, NAP |
Interfaces
9 interfaces between chains.
- E–F · 4057 Ų buried · 31 hydrogen bonds · protein-protein
- A–B · 4048 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 4011 Ų buried · 28 hydrogen bonds · protein-protein
- C–E · 497 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 463 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 3EAN · Crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with reduced… · 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 O89049
- Elsewhere: RCSB PDB 3EAN · PDBe 3EAN · UniProt O89049
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