Research workbench
Structure of the complex between the F360L ppargamma mutant and the ligand LT175 (space group I222)
Analyse Structure of the complex between the F360L ppargamma mutant and the ligand… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L96
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisome proliferator-activated receptor gamma
- UniProt
- P37231
- Ligands
- LRG
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome proliferator-activated receptor gamma | protein | 260 | 70% helix, 5% strand | P37231 |
Ligands and binding sites
- LRG · (2S)-2-(biphenyl-4-yloxy)-3-phenylpropanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 719 | 0.79 | 0.83 | 59 | LRG |
Compared structures
- 4L96 · Structure of the complex between the F360L PPARgamma mutant and the ligand LT175 (space… · 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 4L96 · PDBe 4L96 · UniProt P37231
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