Research workbench
X-ray structure of trypanothione reductase from leishmania infantum in complex with 2-(DIETHYLAMINO)ETHYL 4-((3-(4-nitrophenyl)-3- OXOPROPYL)AMINO)BENZOATE
Analyse X-ray structure of trypanothione reductase from leishmania infantum in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ER5
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypanothione reductase
- EC
- 1.8.1.12
- UniProt
- A4HSF7
- Ligands
- FAD, BVN, SO4
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypanothione reductase (EC 1.8.1.12) | protein | 488 | 32% helix, 25% strand | A4HSF7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- BVN · 2-(diethylamino)ethyl 4-((3-(4-nitrophenyl)-3-oxopropyl)amino)benzoate · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 822 | 0.78 | 0.81 | 97 | FAD, SO4 |
| 2 | 99 | 0.35 | 0.74 | 25 | empty |
| 3 | 72 | 0.34 | 0.76 | 17 | empty |
| 4 | 82 | 0.34 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6ER5 · X-ray structure of Trypanothione Reductase from Leishmania infantum in complex with… · 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 A4HSF7
- Elsewhere: RCSB PDB 6ER5 · PDBe 6ER5 · UniProt A4HSF7
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