scPDB - 1exa entry

Protein Data Bank Entry:

PDB ID : 1exa

Resolution :1.590 Å

Experimental Method : X-ray

Deposition Date : 2000-05-02

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Retinoic acid receptor gamma
ID:	RARG_HUMAN
AC:	P13631
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:	21.562
Number of residues:	43
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.882	509.625

% Hydrophobic	% Polar
75.50	24.50
According to VolSite

Ligand :

HET Code:	394
Formula:	C23H25FNO4
Molecular weight:	398.447 g/mol
DrugBank ID:	DB07031
Buried Surface Area:	83.54 %
Polar Surface area:	89.46 Å2

Number of
H-Bond Acceptors:	4
H-Bond Donors:	2
Rings:	3
Aromatic rings:	2
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	4

Mass center Coordinates

X	Y	Z
39.8011	15.0457	84.3841

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
C20	CH2	TRP- 227	4.23	0	Hydrophobic	false
C18	CE2	PHE- 230	3.88	0	Hydrophobic	false
F1	CE1	PHE- 230	3.53	0	Hydrophobic	false
C20	CE2	PHE- 230	4.07	0	Hydrophobic	false
C11	CB	ALA- 234	4.35	0	Hydrophobic	false
F1	CB	ALA- 234	3.35	0	Hydrophobic	false
C2	CB	CYS- 237	3.88	0	Hydrophobic	false
C4	SG	CYS- 237	3.63	0	Hydrophobic	false
C21	CD1	LEU- 268	4.5	0	Hydrophobic	false
C11	CD1	LEU- 268	4	0	Hydrophobic	false
C5	CD2	LEU- 271	4.06	0	Hydrophobic	false
C22	CB	LEU- 271	4.46	0	Hydrophobic	false
C1	CD2	LEU- 271	4.08	0	Hydrophobic	false
C10	CD1	LEU- 271	4.05	0	Hydrophobic	false
N6	O	LEU- 271	3.15	121.33	H-Bond (Ligand Donor)	false
C19	CE	MET- 272	3.92	0	Hydrophobic	false
C22	SD	MET- 272	3.84	0	Hydrophobic	false
C8	CE	MET- 272	4	0	Hydrophobic	false
C5	CB	ARG- 274	4.01	0	Hydrophobic	false
C5	CB	ILE- 275	3.52	0	Hydrophobic	false
C22	CG2	ILE- 275	4.07	0	Hydrophobic	false
C4	CD1	ILE- 275	4.11	0	Hydrophobic	false
O72	NH1	ARG- 278	3.18	141.22	H-Bond (Protein Donor)	false
O72	CZ	ARG- 278	3.98	0	Ionic (Protein Cationic)	false
F1	CE2	PHE- 288	4.06	0	Hydrophobic	false
C2	CD2	PHE- 288	3.44	0	Hydrophobic	false
O71	N	SER- 289	2.92	166.5	H-Bond (Protein Donor)	false
C18	CD1	PHE- 304	3.82	0	Hydrophobic	false
C19	CD2	PHE- 304	4.45	0	Hydrophobic	false
C22	CZ	PHE- 304	3.71	0	Hydrophobic	false
C19	CD2	LEU- 307	3.8	0	Hydrophobic	false
C15	CG	ARG- 396	4.31	0	Hydrophobic	false
C19	CG	ARG- 396	4.39	0	Hydrophobic	false
C21	CB	ALA- 397	4.19	0	Hydrophobic	false
C14	CB	ALA- 397	4.3	0	Hydrophobic	false
C14	CD2	LEU- 400	3.82	0	Hydrophobic	false
C14	CE	MET- 408	4.49	0	Hydrophobic	false
C20	CG2	ILE- 412	3.82	0	Hydrophobic	false
C21	CG2	ILE- 412	4.09	0	Hydrophobic	false
C21	CE	MET- 415	3.89	0	Hydrophobic	false
C21	CD2	LEU- 416	4.19	0	Hydrophobic	false