scPDB - 2ath entry

Protein Data Bank Entry:

PDB ID : 2ath

Resolution :2.280 Å

Experimental Method : X-ray

Deposition Date : 2005-08-25

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:	25.962
Number of residues:	36
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.757	1805.625

% Hydrophobic	% Polar
55.89	44.11
According to VolSite

Ligand :

HET Code:	3EA
Formula:	C24H22F3N2O5
Molecular weight:	475.437 g/mol
DrugBank ID:	DB07053
Buried Surface Area:	70.43 %
Polar Surface area:	89.55 Å2

Number of
H-Bond Acceptors:	5
H-Bond Donors:	0
Rings:	4
Aromatic rings:	4
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
18.0751	6.74618	37.2005

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
F34	CG2	ILE- 281	3.67	0	Hydrophobic	false
C12	CB	CYS- 285	4.16	0	Hydrophobic	false
F34	SG	CYS- 285	4.49	0	Hydrophobic	false
C17	SG	CYS- 285	4.08	0	Hydrophobic	false
C8	SG	CYS- 285	3.68	0	Hydrophobic	false
C21	CB	CYS- 285	3.47	0	Hydrophobic	false
C28	CG	GLN- 286	4.15	0	Hydrophobic	false
C13	CG	ARG- 288	3.86	0	Hydrophobic	false
C13	CB	SER- 289	4.45	0	Hydrophobic	false
C23	CB	SER- 289	4.26	0	Hydrophobic	false
C28	CB	SER- 289	3.78	0	Hydrophobic	false
O31	OG	SER- 289	3.01	168.45	H-Bond (Protein Donor)	false
O31	NE2	HIS- 323	2.54	161.15	H-Bond (Protein Donor)	false
C13	CG2	ILE- 326	3.95	0	Hydrophobic	false
C13	CD2	LEU- 330	4.35	0	Hydrophobic	false
C11	CD1	LEU- 330	3.84	0	Hydrophobic	false
C16	CD2	LEU- 330	3.8	0	Hydrophobic	false
C15	CE	MET- 334	4.12	0	Hydrophobic	false
C8	CG1	VAL- 339	4.11	0	Hydrophobic	false
C1	CG2	ILE- 341	4.45	0	Hydrophobic	false
F33	CD1	ILE- 341	3.56	0	Hydrophobic	false
C6	CG2	ILE- 341	3.87	0	Hydrophobic	false
F33	CE	MET- 348	3.44	0	Hydrophobic	false
C7	SD	MET- 348	4.31	0	Hydrophobic	false
C7	CD2	LEU- 353	4.14	0	Hydrophobic	false
C8	CD1	LEU- 353	3.94	0	Hydrophobic	false
C15	CD1	LEU- 353	4.4	0	Hydrophobic	false
C20	CB	PHE- 363	4.47	0	Hydrophobic	false
C20	SD	MET- 364	4.27	0	Hydrophobic	false
C17	SD	MET- 364	3.84	0	Hydrophobic	false
C16	CG	LYS- 367	4.1	0	Hydrophobic	false
O30	NE2	HIS- 449	2.8	125.43	H-Bond (Protein Donor)	false
C28	CD1	LEU- 469	4.33	0	Hydrophobic	false
O31	OH	TYR- 473	3.45	150.42	H-Bond (Protein Donor)	false
O30	OH	TYR- 473	2.53	149.23	H-Bond (Protein Donor)	false