MolNFT v1 · #18475 · protein

Human lxr beta hormone receptor / GW3965 complex

1PQ6 · Oxysterols receptor lxr-beta: “Human lxr beta hormone receptor / GW3965 complex”. X-ray diffraction, 1 ligand (965), 11 pockets (best druggability 0.87). MolNFT v1 #18475 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1PQ6
Type: protein
Length: 908 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxysterols receptor lxr-beta
UniProt: P55055
Ligands: 965
Pockets: 11 · best druggability 0.87

Structure

x-ray diffraction · 4 distinct chains · 69% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxysterols receptor lxr-beta	protein	232	70% helix, 4% strand	P55055
B	Oxysterols receptor lxr-beta	protein	241	71% helix, 4% strand	P55055
C	Oxysterols receptor lxr-beta	protein	208	67% helix, 5% strand	P55055
D	Oxysterols receptor lxr-beta	protein	227	68% helix, 4% strand	P55055

Ligands and binding sites

965 · [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid · ligand · 3 copies · chains A, B, D
IPA · Isopropyl alcohol · additive · 2 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.87	0.95	42	965, IPA
2	345	0.86	0.95	42	965
3	398	0.84	0.92	48	965, IPA
4	1044	0.80	0.81	94	empty
5	1071	0.78	0.80	105	empty

Interfaces

2 interfaces between chains.

A–B · 1100 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 1094 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1PQ6 · Human lxr beta hormone receptor / GW3965 complex · the same entry in another collection · chain D against D, TM-score 1.00
P55055 · AlphaFold monomer V2.0 prediction for oxysterols receptor lxr-beta (P55055) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 1PQ6 · PDBe 1PQ6 · UniProt P55055

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