scPDB - 2hfp entry

Protein Data Bank Entry:

PDB ID : 2hfp

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2006-06-25

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:	26.545
Number of residues:	41
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.488	1984.500

% Hydrophobic	% Polar
63.27	36.73
According to VolSite

Ligand :

HET Code:	NSI
Formula:	C30H23F3N2O4S
Molecular weight:	564.575 g/mol
DrugBank ID:	-
Buried Surface Area:	69 %
Polar Surface area:	85.78 Å2

Number of
H-Bond Acceptors:	4
H-Bond Donors:	1
Rings:	5
Aromatic rings:	5
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
22.2244	-10.8696	3.6167

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
O16	O	HOH- 56	2.6	179.99	H-Bond (Protein Donor)	false
C28	CD1	LEU- 255	3.91	0	Hydrophobic	false
C28	CG	GLU- 259	3.3	0	Hydrophobic	false
C28	CD1	ILE- 262	4.33	0	Hydrophobic	false
C54	CD1	ILE- 262	3.98	0	Hydrophobic	false
O52	NZ	LYS- 265	3.26	152.01	H-Bond (Protein Donor)	false
O50	NZ	LYS- 265	2.58	124.98	H-Bond (Protein Donor)	false
C1	CG2	ILE- 281	3.98	0	Hydrophobic	false
C20	CG2	ILE- 281	4.29	0	Hydrophobic	false
C20	SG	CYS- 285	4.11	0	Hydrophobic	false
C38	CB	CYS- 285	4.25	0	Hydrophobic	false
C1	SG	CYS- 285	3.28	0	Hydrophobic	false
C56	CB	PHE- 287	4.2	0	Hydrophobic	false
C55	CB	ARG- 288	4.17	0	Hydrophobic	false
C34	CG	ARG- 288	3.56	0	Hydrophobic	false
F45	CB	ALA- 292	3.45	0	Hydrophobic	false
F46	CG2	ILE- 326	4.4	0	Hydrophobic	false
F45	CG2	ILE- 326	3.83	0	Hydrophobic	false
C35	CG2	ILE- 326	4.35	0	Hydrophobic	false
F45	CE	MET- 329	3.78	0	Hydrophobic	false
F46	CB	MET- 329	3.72	0	Hydrophobic	false
F46	CB	LEU- 330	3.89	0	Hydrophobic	false
C2	CD1	LEU- 330	4.15	0	Hydrophobic	false
C36	CD1	LEU- 330	4.03	0	Hydrophobic	false
C12	CD1	LEU- 333	4.49	0	Hydrophobic	false
F47	CD1	LEU- 333	3.72	0	Hydrophobic	false
C2	CG2	VAL- 339	3.93	0	Hydrophobic	false
C5	CG1	VAL- 339	3.77	0	Hydrophobic	false
C6	CG2	ILE- 341	4.04	0	Hydrophobic	false
C19	CD1	ILE- 341	3.7	0	Hydrophobic	false
O50	N	SER- 342	3.26	123.6	H-Bond (Protein Donor)	false
O16	N	SER- 342	3.13	150.75	H-Bond (Protein Donor)	false
C1	CE	MET- 348	4.26	0	Hydrophobic	false
C19	CE	MET- 348	3.95	0	Hydrophobic	false
C4	CD2	LEU- 353	3.9	0	Hydrophobic	false
C5	CE	MET- 364	3.94	0	Hydrophobic	false