Research workbench
Crystal structure of putative thioredoxin reductase from haemophilus influenzae
Analyse Crystal structure of putative thioredoxin reductase from haemophilus influenzae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U63
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase
- EC
- 1.8.1.9
- UniProt
- P43788
- Ligands
- FAD, NAP, NA
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin reductase (EC 1.8.1.9) | protein | 315 | 30% helix, 29% strand | P43788 |
| B | Thioredoxin reductase (EC 1.8.1.9) | protein | 319 | 29% helix, 29% strand | P43788 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · chains B
- GOL · Glycerol · additive · 6 copies · chains A, B
- ACT · Acetate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.83 | 0.96 | 40 | GOL |
| 2 | 893 | 0.80 | 0.82 | 92 | FAD, ACT, NAP |
| 3 | 954 | 0.79 | 0.81 | 99 | FAD, ACT, NAP |
Interfaces
1 interface between chains.
- A–B · 2391 Ų buried · 53 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5U63 · Crystal structure of putative thioredoxin reductase from Haemophilus influenzae · the same entry in another collection · chain A against A, TM-score 1.00
- P43788 · AlphaFold monomer V2.0 prediction for thioredoxin reductase (P43788) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P43788
- Elsewhere: RCSB PDB 5U63 · PDBe 5U63 · UniProt P43788
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