scPDB - 1i7i entry

Protein Data Bank Entry:

PDB ID : 1i7i

Resolution :2.350 Å

Experimental Method : X-ray

Deposition Date : 2001-03-09

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	7.750	7.750	7.750	0.000	7.750	1

List of CHEMBLId :

CHEMBL282686

Binding Site :

Uniprot Annotation

Name:	Peroxisome proliferator-activated receptor gamma
ID:	PPARG_HUMAN
AC:	P37231
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:	48.462
Number of residues:	35
Including
Standard Amino Acids:	34
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.611	1096.875

% Hydrophobic	% Polar
62.46	37.54
According to VolSite

Ligand :

HET Code:	AZ2
Formula:	C20H23O7S
Molecular weight:	407.457 g/mol
DrugBank ID:	DB06536
Buried Surface Area:	65.93 %
Polar Surface area:	110.34 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	0
Rings:	2
Aromatic rings:	2
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
18.3393	18.6059	13.384

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
C38	CG2	ILE- 281	4.44	0	Hydrophobic	false
C11	CE1	PHE- 282	3.57	0	Hydrophobic	false
C29	SG	CYS- 285	3.99	0	Hydrophobic	false
C8	CB	CYS- 285	3.56	0	Hydrophobic	false
C21	SG	CYS- 285	3.7	0	Hydrophobic	false
C19	CB	CYS- 285	3.99	0	Hydrophobic	false
C36	SG	CYS- 285	3.78	0	Hydrophobic	false
C8	CG	GLN- 286	3.7	0	Hydrophobic	false
C24	CG	ARG- 288	4.44	0	Hydrophobic	false
C41	CB	ARG- 288	4.35	0	Hydrophobic	false
O16	OG	SER- 289	2.82	166.52	H-Bond (Protein Donor)	false
C26	CB	SER- 289	3.81	0	Hydrophobic	false
C5	CB	SER- 289	3.93	0	Hydrophobic	false
O16	NE2	HIS- 323	2.78	158.18	H-Bond (Protein Donor)	false
C26	CG2	ILE- 326	4.07	0	Hydrophobic	false
C2	CE1	TYR- 327	4.23	0	Hydrophobic	false
C29	CD1	LEU- 330	4.2	0	Hydrophobic	false
C23	CD2	LEU- 330	4.22	0	Hydrophobic	false
C32	CG2	VAL- 339	3.87	0	Hydrophobic	false
C35	CG2	ILE- 341	3.78	0	Hydrophobic	false
C38	SD	MET- 348	4.34	0	Hydrophobic	false
C11	CE1	PHE- 363	4.28	0	Hydrophobic	false
C21	SD	MET- 364	3.87	0	Hydrophobic	false
C29	CE	MET- 364	3.6	0	Hydrophobic	false
O7	NE2	HIS- 449	3.23	121.36	H-Bond (Protein Donor)	false
O18	NE2	HIS- 449	2.74	127.35	H-Bond (Protein Donor)	false
C11	CD1	LEU- 453	4.33	0	Hydrophobic	false
O18	OH	TYR- 473	2.7	159.98	H-Bond (Protein Donor)	false