Research workbench
Crystal structure of human ppargamma ligand binding domain in complex with SR16832
Analyse Crystal structure of human ppargamma ligand binding domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AUG
- Type
- protein
- Length
- 522 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisome proliferator-activated receptor gamma
- UniProt
- P37231
- Ligands
- BXG, KNA
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome proliferator-activated receptor gamma | protein | 260 | 67% helix, 4% strand | P37231 |
| B | Peroxisome proliferator-activated receptor gamma | protein | 262 | 62% helix, 5% strand | P37231 |
Ligands and binding sites
- BXG · 2-chloro-N-(6-methoxyquinolin-4-yl)-5-nitrobenzamide · ligand · 2 copies · chains A, B
- KNA · nonanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.84 | 0.90 | 55 | BXG |
| 2 | 395 | 0.78 | 0.87 | 54 | BXG, KNA |
| 3 | 336 | 0.61 | 0.78 | 37 | empty |
| 4 | 356 | 0.60 | 0.77 | 26 | empty |
| 5 | 179 | 0.59 | 0.81 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 977 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6AUG · Crystal Structure of Human PPARgamma Ligand Binding Domain in Complex with SR16832 · 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 6AUG · PDBe 6AUG · UniProt P37231
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