Research workbench
Barley NADPH-dependent thioredoxin reductase 2
Analyse Barley NADPH-dependent thioredoxin reductase 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WHD
- Type
- protein
- Length
- 637 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase
- EC
- 1.8.1.9
- UniProt
- A9LN30
- Ligands
- FAD
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin reductase (EC 1.8.1.9) | protein | 318 | 27% helix, 28% strand | A9LN30 |
| B | Thioredoxin reductase (EC 1.8.1.9) | protein | 319 | 27% helix, 28% strand | A9LN30 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- FLC · Citrate anion · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1162 | 0.85 | 0.86 | 145 | FAD, FLC |
| 2 | 235 | 0.62 | 0.81 | 26 | empty |
| 3 | 247 | 0.60 | 0.80 | 26 | empty |
| 4 | 263 | 0.56 | 0.77 | 35 | FLC |
| 5 | 121 | 0.50 | 0.80 | 20 | FLC |
Interfaces
1 interface between chains.
- A–B · 1189 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2WHD · Barley NADPH-dependent thioredoxin reductase 2 · 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 A9LN30
- Elsewhere: RCSB PDB 2WHD · PDBe 2WHD · UniProt A9LN30
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