Research workbench
Ppar gamma mutant complex
Analyse Ppar gamma mutant complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FZJ
- Type
- protein
- Length
- 559 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisome proliferator-activated receptor gamma; Peroxisome proliferator-activated…
- UniProt
- P37231
- Ligands
- EDK, CL, IOD
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome proliferator-activated receptor gamma | protein | 267 | 68% helix, 5% strand | P37231 |
| B | Peroxisome proliferator-activated receptor gamma | protein | 270 | 70% helix, 5% strand | P37231 |
| C, D | Peroxisome proliferator-activated receptor gamma coactivator 1-alpha | protein | 11 | 64% helix, 0% strand | — |
Ligands and binding sites
- EDK · (2~{S})-3-[4-[2-[methyl(pyridin-2-yl) amino]ethoxy]phenyl]-2-[[2-(phenylcarbonyl) phenyl]amino]propanoic acid · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, B
- IOD · Iodide ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.86 | 0.93 | 57 | EDK, IOD |
| 2 | 412 | 0.85 | 0.93 | 56 | EDK, IOD |
| 3 | 360 | 0.63 | 0.78 | 34 | empty |
| 4 | 328 | 0.61 | 0.78 | 27 | empty |
| 5 | 109 | 0.45 | 0.78 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 764 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 562 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 540 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6FZJ · PPAR gamma mutant complex · 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 6FZJ · PDBe 6FZJ · UniProt P37231
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