Research workbench
Crystal structure of trypanothione reductase from trypanosoma brucei in complex with inhibitor EP127 (5-{5-[1-(pyrrolidin-1-yl) cyclohexyl]-1,3-thiazol-2-yl}-1H-indole)
Analyse Crystal structure of trypanothione reductase from trypanosoma brucei in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NEV
- Type
- protein
- Length
- 970 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypanothione reductase
- EC
- 1.8.1.12
- UniProt
- Q389T8
- Ligands
- 2JR, FAD, SO4
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypanothione reductase (EC 1.8.1.12) | protein | 485 | 32% helix, 26% strand | Q389T8 |
| B | Trypanothione reductase (EC 1.8.1.12) | protein | 485 | 33% helix, 28% strand | Q389T8 |
Ligands and binding sites
- 2JR · 5-{5-[1-(pyrrolidin-1-yl)cyclohexyl]-1,3-thiazol-2-yl}-1H-indole · ligand · 3 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 8 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1071 | 0.85 | 0.85 | 98 | empty |
| 2 | 902 | 0.81 | 0.83 | 105 | FAD, SO4 |
| 3 | 847 | 0.80 | 0.83 | 95 | FAD, SO4 |
| 4 | 653 | 0.69 | 0.77 | 59 | empty |
| 5 | 50 | 0.41 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 3325 Ų buried · 31 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4NEV · Crystal structure of Trypanothione Reductase from Trypanosoma brucei in complex with… · 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 Q389T8
- Elsewhere: RCSB PDB 4NEV · PDBe 4NEV · UniProt Q389T8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.