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Crystal structure of the human pparg-LBD/ROSIGLITAZONE complex obtained by dry co-crystallization and in situ diffraction

Analyse Crystal structure of the human pparg-LBD/ROSIGLITAZONE complex obtained by dry… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XLD
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxisome proliferator-activated receptor gamma
UniProt: P37231
Ligands: BRL
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peroxisome proliferator-activated receptor gamma	protein	263	67% helix, 5% strand	P37231

Ligands and binding sites

BRL · 2,4-thiazolidiinedione, 5-[[4-[2-(methyl-2-pyridinylamino)ethoxy]phenyl]methyl]-(9CL) · ligand · chains A
FMT · Formic acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	492	0.78	0.85	54	BRL
2	59	0.35	0.78	15	empty
3	57	0.28	0.73	13	FMT

Compared structures

4XLD · Crystal structure of the human PPARg-LBD/rosiglitazone complex obtained by dry… · 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 4XLD · PDBe 4XLD · UniProt P37231

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