Research workbench
AlphaFold monomer V2.0 prediction for trypanothione reductase (P39050)
Analyse AlphaFold monomer V2.0 prediction for trypanothione reductase (P39050) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P39050
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Trypanothione reductase
- UniProt
- P39050
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypanothione reductase | protein | 491 | 34% helix, 27% strand | P39050 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1028 | 0.79 | 0.81 | 111 | empty |
| 2 | 85 | 0.32 | 0.73 | 18 | empty |
| 3 | 74 | 0.32 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P39050
- Elsewhere: UniProt P39050 · AlphaFold DB P39050
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