MolNFT v1 · #190103 · protein

X-ray structure of human ppar gamma ligand binding domain-fenofibric acid co-crystals obtained by co-crystallization

7WGP · Isoform 1 of peroxisome proliferator-activated receptor…: “X-ray structure of human ppar gamma ligand binding domain-fenofibric acid co-crystals obtained by…”. X-ray diffraction, 1 ligand (F5A), 1 pocket (best druggability 0.84).…

PDB: 7WGP
Type: protein
Length: 280 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 1 of peroxisome proliferator-activated receptor gamma; 15-meric peptide from…
EC: 2.3.1.48
UniProt: Q15788
Ligands: F5A
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 65% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isoform 1 of peroxisome proliferator-activated receptor gamma	protein	269	65% helix, 4% strand	—
B	15-meric peptide from nuclear receptor coactivator 1 (EC 2.3.1.48)	protein	11	64% helix, 0% strand	Q15788

Ligands and binding sites

F5A · 2-[4-(4-chlorobenzene-1-carbonyl)phenoxy]-2-methylpropanoic acid · ligand · 3 copies · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	877	0.84	0.86	69	F5A

Interfaces

1 interface between chains.

A–B · 633 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7WGP · X-ray structure of human PPAR gamma ligand binding domain-fenofibric acid co-crystals… · 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 Q15788
Elsewhere: RCSB PDB 7WGP · PDBe 7WGP · UniProt Q15788

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