MolNFT v2 · #50961 · protein
X-ray structure of trypanothione reductase from crithidia fasciculata at 2.4 ångströms resolution
2TPR: “X-ray structure of trypanothione reductase from crithidia fasciculata at 2.4 ångströms resolution”. X-ray diffraction at 2.4, 1 ligand (FAD), 8 pockets (best druggability 0.86). MolNFT v2 #50961 on GenesisL1: 3D structure, binding…
- PDB
- 2TPR
- Type
- protein
- Length
- 964 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Crithidia fasciculata
- Molecule
- Trypanothione reductase
- EC
- 1.6.4.8
- UniProt
- P39040
- Ligands
- FAD
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · resolution 2.4 · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trypanothione reductase (EC 1.6.4.8) | protein | 482 | 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
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.86 | 0.87 | 75 | empty |
| 2 | 773 | 0.80 | 0.83 | 96 | FAD |
| 3 | 750 | 0.79 | 0.83 | 96 | FAD |
| 4 | 173 | 0.55 | 0.80 | 29 | empty |
| 5 | 175 | 0.55 | 0.80 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 3240 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2TPR · X-ray structure of trypanothione reductase from crithidia fasciculata at 2.4 ångströms… · 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 A against A, TM-score 0.99
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 2TPR · PDBe 2TPR · UniProt P39040
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