Research workbench
The structure of trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state
Analyse The structure of trypanosoma cruzi trypanothione reductase in the oxidized and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NDA
- Type
- protein
- Length
- 1,924 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypanothione oxidoreductase
- UniProt
- P28593
- Ligands
- FAD
- Pockets
- 14 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Trypanothione oxidoreductase | protein | 481 | 31% helix, 26% strand | P28593 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 999 | 0.86 | 0.87 | 92 | empty |
| 2 | 946 | 0.86 | 0.87 | 76 | empty |
| 3 | 983 | 0.81 | 0.83 | 117 | FAD |
| 4 | 742 | 0.80 | 0.84 | 85 | FAD |
| 5 | 729 | 0.80 | 0.84 | 84 | FAD |
Interfaces
3 interfaces between chains.
- A–B · 3215 Ų buried · 35 hydrogen bonds · protein-protein
- C–D · 3213 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 316 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1NDA · The structure of trypanosoma cruzi trypanothione reductase in the oxidized and NADPH… · the same entry in another collection · chain A against A, TM-score 1.00
- P28593 · AlphaFold monomer V2.0 prediction for trypanothione reductase (P28593) · a predicted model of the same protein · 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 P28593
- Elsewhere: RCSB PDB 1NDA · PDBe 1NDA · UniProt P28593
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.