scPDB - 2pob entry

Protein Data Bank Entry:

PDB ID : 2pob

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2007-04-26

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	6.860	6.860	6.860	0.000	6.860	1

List of CHEMBLId :

CHEMBL230259

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:	78.099
Number of residues:	44
Including
Standard Amino Acids:	44
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.281	1491.750

% Hydrophobic	% Polar
61.09	38.91
According to VolSite

Ligand :

HET Code:	GW4
Formula:	C36H35N3O4
Molecular weight:	573.681 g/mol
DrugBank ID:	-
Buried Surface Area:	64.72 %
Polar Surface area:	93.46 Å2

Number of
H-Bond Acceptors:	5
H-Bond Donors:	2
Rings:	5
Aromatic rings:	5
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
65.6531	33.1195	13.7896

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
C27	CG2	ILE- 281	4.44	0	Hydrophobic	false
C9	CG1	ILE- 281	4.36	0	Hydrophobic	false
C29	CD2	PHE- 282	3.24	0	Hydrophobic	false
C28	CB	PHE- 282	3.64	0	Hydrophobic	false
C3	SG	CYS- 285	3.5	0	Hydrophobic	false
C32	SG	CYS- 285	4.11	0	Hydrophobic	false
C16	SG	CYS- 285	3.66	0	Hydrophobic	false
C18	SG	CYS- 285	3.66	0	Hydrophobic	false
C20	CB	CYS- 285	3.69	0	Hydrophobic	false
C26	CB	CYS- 285	4.25	0	Hydrophobic	false
C22	CB	GLN- 286	3.67	0	Hydrophobic	false
C32	CG	ARG- 288	4.25	0	Hydrophobic	false
C10	CB	SER- 289	4.49	0	Hydrophobic	false
C24	CB	SER- 289	4.02	0	Hydrophobic	false
C35	CD1	ILE- 326	3.63	0	Hydrophobic	false
C15	CG2	ILE- 326	3.75	0	Hydrophobic	false
C12	CE1	TYR- 327	3.7	0	Hydrophobic	false
C16	CD2	LEU- 330	4.21	0	Hydrophobic	false
C18	CD1	LEU- 330	4.2	0	Hydrophobic	false
C32	CD1	LEU- 330	4.03	0	Hydrophobic	false
C3	CG1	VAL- 339	4.05	0	Hydrophobic	false
C33	CG2	VAL- 339	4.36	0	Hydrophobic	false
C4	CG2	ILE- 341	4.03	0	Hydrophobic	false
C33	CG2	ILE- 341	4.02	0	Hydrophobic	false
C5	CD1	ILE- 341	3.92	0	Hydrophobic	false
C9	CE	MET- 348	3.82	0	Hydrophobic	false
C3	CD1	LEU- 353	4.24	0	Hydrophobic	false
C26	CE2	PHE- 363	3.02	0	Hydrophobic	false
C3	CE	MET- 364	4.08	0	Hydrophobic	false
C16	CE	MET- 364	3.35	0	Hydrophobic	false
C29	CD2	LEU- 452	4.41	0	Hydrophobic	false
C22	CD1	LEU- 465	4.31	0	Hydrophobic	false
C23	CD1	LEU- 469	3.56	0	Hydrophobic	false
C35	CE2	TYR- 473	4.44	0	Hydrophobic	false
O3	OH	TYR- 473	3.46	134.59	H-Bond (Protein Donor)	false