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Lxrbeta ligand binding domain in complex with small molecule inhibitors

Analyse Lxrbeta ligand binding domain in complex with small molecule inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6S5K
Type: protein
Length: 223 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxysterols receptor lxr-beta
UniProt: P55055
Ligands: KWE
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxysterols receptor lxr-beta	protein	223	72% helix, 3% strand	P55055

Ligands and binding sites

KWE · 3-(4-phenylbutylamino)-1,4-bis(phenylmethyl)pyrrole-2, 5-dione · ligand · 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	278	0.82	0.93	37	KWE
2	94	0.37	0.75	16	empty
3	92	0.37	0.76	21	empty

Compared structures

6S5K · LXRbeta ligand binding domain in complex with small molecule inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
P55055 · AlphaFold monomer V2.0 prediction for oxysterols receptor lxr-beta (P55055) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P55055
Elsewhere: RCSB PDB 6S5K · PDBe 6S5K · UniProt P55055

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