Research workbench
Targeting the PEX14-PEX5 interaction by small molecules provides novel therapeutic routes to treat trypanosomiases.
Analyse Targeting the PEX14-PEX5 interaction by small molecules provides novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L87
- Type
- protein
- Length
- 62 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 0.87
- Source
- Trypanosoma brucei brucei
- Molecule
- Peroxin 14
- UniProt
- Q8IEW2
- Ligands
- 6RD
Structure
x-ray diffraction · resolution 0.87 · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxin 14 | protein | 62 | 68% helix, 0% strand | Q8IEW2 |
Ligands and binding sites
- 6RD · 5-(1~{H}-indol-3-ylmethyl)-1-methyl-~{N}-(naphthalen-1-ylmethyl)-6,7-dihydro-4~{H}-pyrazolo[4,3-c]pyridine-3-carboxamide · ligand · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5L87 · Targeting the PEX14-PEX5 interaction by small molecules provides novel therapeutic routes… · 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 Q8IEW2
- Elsewhere: RCSB PDB 5L87 · PDBe 5L87 · UniProt Q8IEW2
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