scPDB - 1ot7 entry

Protein Data Bank Entry:

PDB ID : 1ot7

Resolution :2.900 Å

Experimental Method : X-ray

Deposition Date : 2003-03-21

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Bile acid receptor
ID:	NR1H4_RAT
AC:	Q62735
Organism:	Rattus norvegicus
Reign:	Eukaryota
TaxID:	10116
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	83.703
Number of residues:	37
Including
Standard Amino Acids:	37
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.686	847.125

% Hydrophobic	% Polar
61.75	38.25
According to VolSite

Ligand :

HET Code:	CHC
Formula:	C26H43O4
Molecular weight:	419.617 g/mol
DrugBank ID:	DB05990
Buried Surface Area:	68.88 %
Polar Surface area:	80.59 Å2

Number of
H-Bond Acceptors:	4
H-Bond Donors:	2
Rings:	4
Aromatic rings:	0
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	5

Mass center Coordinates

X	Y	Z
12.9032	37.2928	16.7089

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
C23	CG	MET- 262	3.78	0	Hydrophobic	false
C18	CG	LEU- 284	4.24	0	Hydrophobic	false
C19	CD2	LEU- 284	4.2	0	Hydrophobic	false
C18	SD	MET- 287	4.39	0	Hydrophobic	false
C21	CB	MET- 287	3.74	0	Hydrophobic	false
C12	CB	ALA- 288	4	0	Hydrophobic	false
C21	CB	HIS- 291	3.65	0	Hydrophobic	false
C23	CB	HIS- 291	4.44	0	Hydrophobic	false
C12	CG	MET- 325	3.87	0	Hydrophobic	false
C14	SD	MET- 325	4.43	0	Hydrophobic	false
C17	CG	MET- 325	4.41	0	Hydrophobic	false
C2	CE	MET- 325	4.08	0	Hydrophobic	false
C9	SD	MET- 325	4.08	0	Hydrophobic	false
C4	CE2	PHE- 326	4.25	0	Hydrophobic	false
OT1	NH2	ARG- 328	2.88	121.22	H-Bond (Protein Donor)	false
OT1	CZ	ARG- 328	3.7	0	Ionic (Protein Cationic)	false
OT2	CZ	ARG- 328	3.59	0	Ionic (Protein Cationic)	false
O7	OG	SER- 329	3.37	141.6	H-Bond (Ligand Donor)	false
C16	CB	SER- 329	4.05	0	Hydrophobic	false
C7	CE1	PHE- 333	4.21	0	Hydrophobic	false
C15	CZ	PHE- 333	3.77	0	Hydrophobic	false
C15	CD2	LEU- 345	4.08	0	Hydrophobic	false
C15	CD1	ILE- 349	4.25	0	Hydrophobic	false
C19	CG2	ILE- 349	4.48	0	Hydrophobic	false
C7	CD1	ILE- 349	3.52	0	Hydrophobic	false
C25	CG2	ILE- 349	3.35	0	Hydrophobic	false
O3	OH	TYR- 358	2.85	149.6	H-Bond (Protein Donor)	false
C3	CE2	TYR- 358	3.94	0	Hydrophobic	false
C25	CB	ILE- 359	4.12	0	Hydrophobic	false
C26	CG	MET- 362	4.26	0	Hydrophobic	false
C25	CE1	PHE- 363	3.46	0	Hydrophobic	false
O7	OH	TYR- 366	3.13	161.03	H-Bond (Protein Donor)	false
C26	CE1	TYR- 366	4.4	0	Hydrophobic	false
O3	ND1	HIS- 444	2.63	155.22	H-Bond (Protein Donor)	false
C1	CH2	TRP- 451	3.88	0	Hydrophobic	false
C19	CH2	TRP- 451	4.08	0	Hydrophobic	false
C11	CH2	TRP- 466	4.38	0	Hydrophobic	false
C2	CH2	TRP- 466	3.7	0	Hydrophobic	false