Research workbench
Trypanosoma brucei trypanothione reductase with NADP and trypanothione bound
Analyse Trypanosoma brucei trypanothione reductase with NADP and trypanothione bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WOW
- Type
- protein
- Length
- 1,959 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypanothione reductase
- EC
- 1.8.1.12
- UniProt
- Q389T8
- Ligands
- FAD, NDP, GCG
- Pockets
- 16 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypanothione reductase (EC 1.8.1.12) | protein | 490 | 33% helix, 28% strand | Q389T8 |
| B | Trypanothione reductase (EC 1.8.1.12) | protein | 488 | 34% helix, 28% strand | Q389T8 |
| C | Trypanothione reductase (EC 1.8.1.12) | protein | 491 | 34% helix, 27% strand | Q389T8 |
| D | Trypanothione reductase (EC 1.8.1.12) | protein | 490 | 33% helix, 27% strand | Q389T8 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- GCG · Bis(gamma-glutamyl-cysteinyl-glycinyl)spermidine · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 702 | 0.86 | 0.90 | 71 | empty |
| 2 | 763 | 0.86 | 0.89 | 70 | empty |
| 3 | 849 | 0.81 | 0.83 | 96 | FAD, NDP |
| 4 | 925 | 0.81 | 0.82 | 104 | FAD, NDP |
| 5 | 853 | 0.80 | 0.83 | 100 | FAD, NDP |
Interfaces
3 interfaces between chains.
- C–D · 3422 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 3415 Ų buried · 33 hydrogen bonds · protein-protein
- B–C · 523 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 2WOW · Trypanosoma brucei trypanothione reductase with NADP and trypanothione bound · 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 2WOW · PDBe 2WOW · UniProt Q389T8
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