Research workbench
Crystal and molecular structure of crithidia fasciculata trypanothione reductase at 2.6 ångströms resolution
Analyse Crystal and molecular structure of crithidia fasciculata trypanothione… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TYT
- Type
- protein
- Length
- 973 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypanothione reductase, oxidized form
- EC
- 1.6.4.8
- UniProt
- P39040
- Ligands
- FAD
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypanothione reductase, oxidized form (EC 1.6.4.8) | protein | 487 | 33% helix, 28% strand | P39040 |
| B | Trypanothione reductase, oxidized form (EC 1.6.4.8) | protein | 486 | 34% helix, 27% strand | P39040 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, 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 | 961 | 0.86 | 0.87 | 71 | empty |
| 2 | 761 | 0.80 | 0.83 | 91 | FAD |
| 3 | 756 | 0.80 | 0.83 | 95 | FAD |
| 4 | 174 | 0.55 | 0.80 | 29 | empty |
| 5 | 89 | 0.49 | 0.82 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 3328 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1TYT · Crystal and molecular structure of crithidia fasciculata trypanothione reductase at 2.6… · the same entry in another collection · chain A against A, TM-score 1.00
- P39040 · AlphaFold monomer V2.0 prediction for trypanothione reductase (P39040) · a predicted model of the same protein · chain B 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 P39040
- Elsewhere: RCSB PDB 1TYT · PDBe 1TYT · UniProt P39040
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