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Human lxr beta hormone receptor complexed with T0901317

Analyse Human lxr beta hormone receptor complexed with T0901317 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PQC
Type: protein
Length: 920 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxysterols receptor lxr-beta
UniProt: P55055
Ligands: 444
Pockets: 16 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 71% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxysterols receptor lxr-beta	protein	232	70% helix, 5% strand	P55055
B	Oxysterols receptor lxr-beta	protein	238	69% helix, 4% strand	P55055
C	Oxysterols receptor lxr-beta	protein	231	69% helix, 4% strand	P55055
D	Oxysterols receptor lxr-beta	protein	219	74% helix, 2% strand	P55055

Ligands and binding sites

444 · N-(2,2,2-trifluoroethyl)-N-{4-[2,2,2-trifluoro-1-hydroxy-1-(trifluoromethyl) ethyl]phenyl}benzenesulfonamide · ligand · 4 copies · chains A, B, C, D

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

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	222	0.85	0.97	25	444
2	225	0.84	0.96	25	444
3	314	0.84	0.94	43	444
4	376	0.84	0.92	37	444
5	1162	0.79	0.81	109	empty

Interfaces

3 interfaces between chains.

C–D · 1100 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 1071 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 150 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1PQC · Human lxr beta hormone receptor complexed with T0901317 · 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 D 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 1PQC · PDBe 1PQC · UniProt P55055

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