scPDB - 1upw entry

Protein Data Bank Entry:

PDB ID : 1upw

Resolution :2.400 Å

Experimental Method : X-ray

Deposition Date : 2003-10-13

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	6.990	6.990	6.990	0.000	6.990	1

List of CHEMBLId :

CHEMBL62136

Binding Site :

Uniprot Annotation

Name:	Oxysterols receptor LXR-beta
ID:	NR1H2_HUMAN
AC:	P55055
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	100 %

Ligand binding site composition:

B-Factor:	10.190
Number of residues:	33
Including
Standard Amino Acids:	33
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.287	789.750

% Hydrophobic	% Polar
61.11	38.89
According to VolSite

Ligand :

HET Code:	444
Formula:	C17H12F9NO3S
Molecular weight:	481.333 g/mol
DrugBank ID:	DB07080
Buried Surface Area:	77.25 %
Polar Surface area:	65.98 Å2

Number of
H-Bond Acceptors:	3
H-Bond Donors:	1
Rings:	2
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
95.3208	-11.717	11.9136

Binding mode :

What is Poseview ?

2D View
3D View

Image generated by PoseView

Protein

Binding Site

Ligand

Interaction pattern

hydrophobic (CA)

aromatic (CZ)

hydrogen bond acceptor (O)

hydrogen bond acceptor/donor (OG)

hydrogen bond donor (N)

positively ionized (NZ)

negatively ionized (OD1)

metal (ZN)

Legend:

Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand

Image generated using PoseView by BioSolveIT

Ligand	Protein		Interaction
Atom	Atom	Residue	Distance (Å)	Angle (°)	Type
F36	CE1	PHE- 268	4.5	0	Hydrophobic	false
F35	CE1	PHE- 268	3.68	0	Hydrophobic	false
F40	CE1	PHE- 268	4.49	0	Hydrophobic	false
F41	CE1	PHE- 268	4.29	0	Hydrophobic	false
F36	CB	PHE- 271	3.64	0	Hydrophobic	false
C04	CD2	PHE- 271	3.5	0	Hydrophobic	false
C03	CB	PHE- 271	4.12	0	Hydrophobic	false
C05	CD1	LEU- 274	3.74	0	Hydrophobic	false
C04	CB	LEU- 274	3.24	0	Hydrophobic	false
F37	CB	ALA- 275	3.53	0	Hydrophobic	false
C02	CB	ALA- 275	4.15	0	Hydrophobic	false
F22	CD1	ILE- 309	4.34	0	Hydrophobic	false
C28	CD1	ILE- 309	3.88	0	Hydrophobic	false
F20	CB	MET- 312	4.33	0	Hydrophobic	false
C02	CE	MET- 312	4.04	0	Hydrophobic	false
C28	CE	MET- 312	3.22	0	Hydrophobic	false
F22	CG	LEU- 313	3.65	0	Hydrophobic	false
F21	CD2	LEU- 313	3.37	0	Hydrophobic	false
O13	OG1	THR- 316	2.52	125.05	H-Bond (Protein Donor)	false
F21	CG2	THR- 316	3.84	0	Hydrophobic	false
F20	CB	THR- 316	4.08	0	Hydrophobic	false
C06	CD1	ILE- 327	3.39	0	Hydrophobic	false
C25	CD1	LEU- 345	4.36	0	Hydrophobic	false
F40	CD2	LEU- 345	3.52	0	Hydrophobic	false
F39	CD1	LEU- 345	4.23	0	Hydrophobic	false
F22	CZ	PHE- 349	3.8	0	Hydrophobic	false
F39	CZ	PHE- 349	3.96	0	Hydrophobic	false
F22	CG1	ILE- 353	3.63	0	Hydrophobic	false
F21	CG1	ILE- 353	3.4	0	Hydrophobic	false
C19	CG2	ILE- 353	3.98	0	Hydrophobic	false
O42	NE2	HIS- 435	2.59	164.86	H-Bond (Protein Donor)	false
F39	CG	GLN- 438	3.83	0	Hydrophobic	false
F41	CG2	VAL- 439	3.59	0	Hydrophobic	false
F41	CD2	LEU- 442	3.32	0	Hydrophobic	false
F35	CG	LEU- 449	4.42	0	Hydrophobic	false
C34	CD2	LEU- 449	4.23	0	Hydrophobic	false
F37	CD1	LEU- 453	4.1	0	Hydrophobic	false
F37	CZ3	TRP- 457	4.34	0	Hydrophobic	false