Research workbench
Chlamydomonas reinhardtii NADPH dependent thioredoxin reductase 1 domain cs mutant
Analyse Chlamydomonas reinhardtii NADPH dependent thioredoxin reductase 1 domain cs… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P9E
- Type
- protein
- Length
- 631 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase
- EC
- 1.8.1.9
- UniProt
- A0A2K3E888
- Ligands
- FAD, P4G
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin reductase (EC 1.8.1.9) | protein | 315 | 25% helix, 28% strand | A0A2K3E888 |
| B | Thioredoxin reductase (EC 1.8.1.9) | protein | 316 | 25% helix, 28% strand | A0A2K3E888 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- P4G · 1-ethoxy-2-(2-ethoxyethoxy)ethane · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 831 | 0.81 | 0.84 | 91 | FAD |
| 2 | 806 | 0.80 | 0.84 | 94 | FAD |
| 3 | 328 | 0.59 | 0.77 | 42 | empty |
| 4 | 58 | 0.46 | 0.84 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2599 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 7P9E · Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domain CS mutant · 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 A0A2K3E888
- Elsewhere: RCSB PDB 7P9E · PDBe 7P9E · UniProt A0A2K3E888
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.