Research workbench
Crystal structure of ppargamma lbd bound to full agonist MRL20
Analyse Crystal structure of ppargamma lbd bound to full agonist MRL20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q59
- Type
- protein
- Length
- 508 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisome proliferator-activated receptor gamma
- UniProt
- P37231
- Ligands
- 240
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome proliferator-activated receptor gamma | protein | 255 | 69% helix, 5% strand | P37231 |
| B | Peroxisome proliferator-activated receptor gamma | protein | 253 | 66% helix, 5% strand | P37231 |
Ligands and binding sites
- 240 · (2S)-2-(2-{[1-(4-methoxybenzoyl)-2-methyl-5-(trifluoromethoxy)-1H-indol-3-yl]methyl}phenoxy)propanoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 772 | 0.81 | 0.84 | 89 | 240 |
| 2 | 470 | 0.79 | 0.86 | 46 | 240 |
| 3 | 520 | 0.70 | 0.79 | 57 | empty |
| 4 | 60 | 0.33 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 962 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (artifact).
Compared structures
- 2Q59 · Crystal Structure of PPARgamma LBD bound to full agonist MRL20 · 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 P37231
- Elsewhere: RCSB PDB 2Q59 · PDBe 2Q59 · UniProt P37231
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.