scPDB - 1zeo entry

Protein Data Bank Entry:

PDB ID : 1zeo

Resolution :2.500 Å

Experimental Method : X-ray

Deposition Date : 2005-04-19

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:	58.600
Number of residues:	39
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.534	1002.375

% Hydrophobic	% Polar
59.26	40.74
According to VolSite

Ligand :

HET Code:	C01
Formula:	C25H30NO5
Molecular weight:	424.509 g/mol
DrugBank ID:	-
Buried Surface Area:	75.89 %
Polar Surface area:	78.9 Å2

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

Mass center Coordinates

X	Y	Z
19.9203	7.11923	15.4764

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
C11	CG2	ILE- 281	3.91	0	Hydrophobic	false
C11	CB	PHE- 282	3.63	0	Hydrophobic	false
C20	CZ	PHE- 282	3.64	0	Hydrophobic	false
C16	CE2	PHE- 282	3.9	0	Hydrophobic	false
C17	CB	CYS- 285	4.23	0	Hydrophobic	false
C3	CB	CYS- 285	3.97	0	Hydrophobic	false
C5	SG	CYS- 285	3.51	0	Hydrophobic	false
C40	CB	CYS- 285	3.48	0	Hydrophobic	false
C20	CB	GLN- 286	3.92	0	Hydrophobic	false
C49	CG	ARG- 288	3.83	0	Hydrophobic	false
C44	CB	SER- 289	4.47	0	Hydrophobic	false
C40	CB	SER- 289	3.33	0	Hydrophobic	false
C40	CB	SER- 289	3.33	0	Hydrophobic	false
O60	OG	SER- 289	2.68	150.99	H-Bond (Protein Donor)	false
C54	CB	ALA- 292	4	0	Hydrophobic	false
O60	NE2	HIS- 323	2.85	153.34	H-Bond (Protein Donor)	false
C43	CG2	ILE- 326	3.31	0	Hydrophobic	false
C54	CG2	ILE- 326	3.49	0	Hydrophobic	false
C30	CE1	TYR- 327	4.29	0	Hydrophobic	false
C50	CD1	LEU- 330	3.5	0	Hydrophobic	false
C11	CD1	PHE- 360	3.68	0	Hydrophobic	false
C11	CD2	PHE- 363	4.1	0	Hydrophobic	false
C16	CZ	PHE- 363	4.17	0	Hydrophobic	false
C6	CB	PHE- 363	3.65	0	Hydrophobic	false
C27	SD	MET- 364	3.21	0	Hydrophobic	false
C27	SD	MET- 364	3.21	0	Hydrophobic	false
C30	CG	LYS- 367	4.17	0	Hydrophobic	false
O61	NE2	HIS- 449	2.65	136.38	H-Bond (Protein Donor)	false
C16	CD2	LEU- 453	4.2	0	Hydrophobic	false
C20	CD2	LEU- 453	4.48	0	Hydrophobic	false
C20	CD1	LEU- 465	4.15	0	Hydrophobic	false
C20	CD1	LEU- 469	4.15	0	Hydrophobic	false
O60	OH	TYR- 473	3.42	151.43	H-Bond (Protein Donor)	false
O61	OH	TYR- 473	2.55	143.13	H-Bond (Protein Donor)	false