scPDB - 3vn2 entry

Protein Data Bank Entry:

PDB ID : 3vn2

Resolution :2.180 Å

Experimental Method : X-ray

Deposition Date : 2011-12-21

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

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:	56.598
Number of residues:	40
Including
Standard Amino Acids:	40
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.594	1154.250

% Hydrophobic	% Polar
62.28	37.72
According to VolSite

Ligand :

HET Code:	TLS
Formula:	C33H29N4O2
Molecular weight:	513.609 g/mol
DrugBank ID:	DB00966
Buried Surface Area:	69.07 %
Polar Surface area:	75.77 Å2

Number of
H-Bond Acceptors:	4
H-Bond Donors:	0
Rings:	6
Aromatic rings:	6
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
45.4444	21.7135	26.876

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
C31	CG2	ILE- 281	4.03	0	Hydrophobic	false
C13	CZ	PHE- 282	4.13	0	Hydrophobic	false
C24	CB	PHE- 282	3.55	0	Hydrophobic	false
C27	CB	PHE- 282	4.01	0	Hydrophobic	false
C21	CB	CYS- 285	4.33	0	Hydrophobic	false
C23	SG	CYS- 285	4.07	0	Hydrophobic	false
C28	SG	CYS- 285	4.02	0	Hydrophobic	false
C9	CB	CYS- 285	3.64	0	Hydrophobic	false
C33	SG	CYS- 285	3.6	0	Hydrophobic	false
C13	CG	GLN- 286	3.79	0	Hydrophobic	false
C10	CB	SER- 289	3.56	0	Hydrophobic	false
C16	CB	SER- 289	4.38	0	Hydrophobic	false
C20	CB	HIS- 323	3.39	0	Hydrophobic	false
C10	CD1	ILE- 326	3.74	0	Hydrophobic	false
C16	CG2	ILE- 326	3.82	0	Hydrophobic	false
C6	CE1	TYR- 327	3.49	0	Hydrophobic	false
C32	CD1	LEU- 330	4.27	0	Hydrophobic	false
C22	CD2	LEU- 330	3.63	0	Hydrophobic	false
C26	CD2	LEU- 330	3.74	0	Hydrophobic	false
C37	CG1	VAL- 339	3.89	0	Hydrophobic	false
C34	CG2	ILE- 341	3.68	0	Hydrophobic	false
C31	CD2	LEU- 353	3.77	0	Hydrophobic	false
C30	CD1	LEU- 356	3.89	0	Hydrophobic	false
C30	CB	PHE- 360	4.31	0	Hydrophobic	false
C24	CE2	PHE- 363	3.44	0	Hydrophobic	false
C30	CB	PHE- 363	3.75	0	Hydrophobic	false
C28	SD	MET- 364	3.84	0	Hydrophobic	false
C29	CE	MET- 364	3.94	0	Hydrophobic	false
C31	CG	MET- 364	3.82	0	Hydrophobic	false
C33	CG	MET- 364	4.11	0	Hydrophobic	false
C22	SD	MET- 364	3.38	0	Hydrophobic	false
C36	CE	MET- 364	3.45	0	Hydrophobic	false
C13	CD1	LEU- 453	3.78	0	Hydrophobic	false
C13	CD1	LEU- 465	3.87	0	Hydrophobic	false
C13	CD1	LEU- 469	4.02	0	Hydrophobic	false
C15	CD2	LEU- 469	4.17	0	Hydrophobic	false
N7	OH	TYR- 473	3.1	175.82	H-Bond (Protein Donor)	false
C20	CZ	TYR- 473	3.4	0	Hydrophobic	false