MolNFT v1 · #15716 · protein
The structure of trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state
1NDA · Trypanothione oxidoreductase: “The structure of trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state”. X-ray diffraction, 1 ligand (FAD), 14 pockets (best druggability 0.86). MolNFT v1 #15716 on…
- 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
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