Research workbench

Crystal structure of human ppargamma ligand binding domain (protein delipidated by denature and refold)

Analyse Crystal structure of human ppargamma ligand binding domain (protein delipidated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VZO
Type: protein
Length: 514 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxisome proliferator-activated receptor gamma
UniProt: P37231
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 66% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peroxisome proliferator-activated receptor gamma	protein	260	64% helix, 5% strand	P37231
B	Peroxisome proliferator-activated receptor gamma	protein	254	68% helix, 5% strand	P37231

Pockets

9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	415	0.81	0.89	52	empty
2	384	0.73	0.84	50	empty
3	506	0.68	0.78	41	empty
4	202	0.57	0.79	24	empty
5	114	0.51	0.82	16	empty

Interfaces

1 interface between chains.

A–B · 914 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6VZO · Crystal structure of human PPARgamma ligand binding domain (Protein delipidated by… · 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 6VZO · PDBe 6VZO · UniProt P37231

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.