MolNFT v1 · #56953 · protein
CYS285SER mutant ppargamma ligand-binding domain complexed with 15- deoxy-DELTA12,14-prostaglandin J2
2ZVT · Peroxisome proliferator-activated receptor gamma: “CYS285SER mutant ppargamma ligand-binding domain complexed with 15- deoxy-DELTA12,14-prostaglandin J2”. X-ray diffraction, 1 ligand (PTG), 8 pockets (best druggability 0.82). MolNFT…
- PDB
- 2ZVT
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisome proliferator-activated receptor gamma
- UniProt
- P37231
- Ligands
- PTG
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome proliferator-activated receptor gamma | protein | 274 | 65% helix, 5% strand | P37231 |
| B | Peroxisome proliferator-activated receptor gamma | protein | 263 | 64% helix, 5% strand | P37231 |
Ligands and binding sites
- PTG · (5E,14E)-11-oxoprosta-5,9,12,14-tetraen-1-oic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 528 | 0.82 | 0.88 | 73 | PTG |
| 2 | 482 | 0.81 | 0.88 | 53 | PTG |
| 3 | 178 | 0.57 | 0.81 | 26 | empty |
| 4 | 121 | 0.55 | 0.83 | 23 | empty |
| 5 | 215 | 0.53 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 928 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2ZVT · Cys285Ser mutant PPARgamma ligand-binding domain complexed with… · 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 2ZVT · PDBe 2ZVT · UniProt P37231
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