scPDB - 3v9v entry

Protein Data Bank Entry:

PDB ID : 3v9v

Resolution :1.600 Å

Experimental Method : X-ray

Deposition Date : 2011-12-28

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:	25.366
Number of residues:	38
Including
Standard Amino Acids:	37
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.428	874.125

% Hydrophobic	% Polar
60.23	39.77
According to VolSite

Ligand :

HET Code:	21L
Formula:	C32H28NO9
Molecular weight:	570.566 g/mol
DrugBank ID:	-
Buried Surface Area:	66.25 %
Polar Surface area:	151.29 Å2

Number of
H-Bond Acceptors:	9
H-Bond Donors:	2
Rings:	5
Aromatic rings:	3
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
11.3693	48.7817	60.3641

Binding mode :

What is Poseview ?

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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
C27	CB	ILE- 262	4.09	0	Hydrophobic	false
O34	NH1	ARG- 280	2.58	126.45	H-Bond (Protein Donor)	false
O36	NH1	ARG- 280	3.31	138.79	H-Bond (Protein Donor)	false
O36	NH2	ARG- 280	3.41	135.65	H-Bond (Protein Donor)	false
C7	CG2	ILE- 281	4.33	0	Hydrophobic	false
C28	CG2	ILE- 281	3.74	0	Hydrophobic	false
C28	SG	CYS- 285	3.39	0	Hydrophobic	false
C8	SG	CYS- 285	3.87	0	Hydrophobic	false
C15	SG	CYS- 285	4.04	0	Hydrophobic	false
C9	SG	CYS- 285	3.7	0	Hydrophobic	false
C6	CB	CYS- 285	3.54	0	Hydrophobic	false
C14	CB	ARG- 288	4.48	0	Hydrophobic	false
C32	CB	SER- 289	3.81	0	Hydrophobic	false
C29	CB	HIS- 323	4.1	0	Hydrophobic	false
C29	CG2	ILE- 326	3.99	0	Hydrophobic	false
C32	CG2	ILE- 326	3.88	0	Hydrophobic	false
C29	CD1	TYR- 327	3.36	0	Hydrophobic	false
C9	CD2	LEU- 330	3.8	0	Hydrophobic	false
C8	CD2	LEU- 330	3.88	0	Hydrophobic	false
C13	CD2	LEU- 330	4.01	0	Hydrophobic	false
C2	CE	MET- 334	3.64	0	Hydrophobic	false
C2	CG1	VAL- 339	4.24	0	Hydrophobic	false
C27	CD1	ILE- 341	4.36	0	Hydrophobic	false
C16	CD1	ILE- 341	4.02	0	Hydrophobic	false
C10	CG2	ILE- 341	3.58	0	Hydrophobic	false
C28	SD	MET- 348	3.93	0	Hydrophobic	false
C7	CE	MET- 348	3.99	0	Hydrophobic	false
C2	CD1	LEU- 353	4.34	0	Hydrophobic	false
C28	CD2	LEU- 353	3.66	0	Hydrophobic	false
C30	CZ	PHE- 363	4.29	0	Hydrophobic	false
C3	SD	MET- 364	3.83	0	Hydrophobic	false
C1	CB	LYS- 367	3.91	0	Hydrophobic	false
C3	CG	LYS- 367	3.6	0	Hydrophobic	false