Research workbench
X-ray structure of human PPARalpha ligand binding domain-GW7647 co-crystals obtained by soaking
Analyse X-ray structure of human PPARalpha ligand binding domain-GW7647 co-crystals… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KAY
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.735
- Source
- Homo sapiens
- Molecule
- Peroxisome proliferator-activated receptor alpha
- UniProt
- Q07869
- Ligands
- 2VN
- Pockets
- 2 · best druggability 0.85
Structure
x-ray diffraction · resolution 1.735 · 1 distinct chain · 68% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome proliferator-activated receptor alpha | protein | 258 | 68% helix, 5% strand | Q07869 |
Ligands and binding sites
- 2VN · 2-[(4-{2-[(4-cyclohexylbutyl)(cyclohexylcarbamoyl) amino]ethyl}phenyl)sulfanyl]-2-methylpropanoic acid · ligand · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 568 | 0.85 | 0.90 | 53 | 2VN |
| 2 | 52 | 0.28 | 0.74 | 10 | empty |
Compared structures
- 6KAY · X-ray structure of human pparalpha ligand binding domain-GW7647 co- crystals obtained by… · the same entry in another collection · chain A against A, TM-score 1.00
- Q07869 · AlphaFold monomer V2.0 prediction for peroxisome proliferator- activated receptor alpha… · 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 Q07869
- Elsewhere: RCSB PDB 6KAY · PDBe 6KAY · UniProt Q07869
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