scPDB - 3frq entry

Protein Data Bank Entry:

PDB ID : 3frq

Resolution :1.760 Å

Experimental Method : X-ray

Deposition Date : 2009-01-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Erythromycin resistance repressor protein
ID:	Q9EVJ6_ECOLX
AC:	Q9EVJ6
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	562
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	97 %
B	3 %

Ligand binding site composition:

B-Factor:	23.585
Number of residues:	38
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:
Metals:	CL

Cavity properties

Ligandability	Volume (Å3)
1.479	1231.875

% Hydrophobic	% Polar
50.96	49.04
According to VolSite

Ligand :

HET Code:	ERY
Formula:	C37H68NO13
Molecular weight:	734.935 g/mol
DrugBank ID:	DB00199
Buried Surface Area:	60.61 %
Polar Surface area:	195.11 Å2

Number of
H-Bond Acceptors:	13
H-Bond Donors:	6
Rings:	3
Aromatic rings:	0
Anionic atoms:	0
Cationic atoms:	1
Rule of Five Violation:	3
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
11.0904	6.47957	21.5245

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
C19	CG2	THR- 17	3.66	0	Hydrophobic	false
C19	CD2	LEU- 20	4.06	0	Hydrophobic	false
C20	CG	LYS- 21	4.1	0	Hydrophobic	false
C19	SD	MET- 59	4.43	0	Hydrophobic	false
C32	CG2	VAL- 66	3.89	0	Hydrophobic	false
C26	CG2	VAL- 66	4.16	0	Hydrophobic	false
C27	CG1	VAL- 66	4.36	0	Hydrophobic	false
C21	CG2	VAL- 66	3.62	0	Hydrophobic	false
C25	CG	TYR- 69	3.93	0	Hydrophobic	false
C27	CD2	TYR- 69	3.9	0	Hydrophobic	false
C33	CD1	LEU- 89	3.75	0	Hydrophobic	false
C27	CD1	LEU- 89	3.69	0	Hydrophobic	false
C25	CB	SER- 92	4.17	0	Hydrophobic	false
C10	SD	MET- 93	4.35	0	Hydrophobic	false
C7	SD	MET- 93	4	0	Hydrophobic	false
C33	SD	MET- 93	4.08	0	Hydrophobic	false
C35	SD	MET- 93	3.71	0	Hydrophobic	false
C37	CB	ASN- 102	4.37	0	Hydrophobic	false
C30	CB	ASN- 102	3.99	0	Hydrophobic	false
C36	CE1	TYR- 103	3.45	0	Hydrophobic	false
C30	CG2	ILE- 105	4.08	0	Hydrophobic	false
C15	CG2	ILE- 105	4.31	0	Hydrophobic	false
C20	CD1	ILE- 105	4.1	0	Hydrophobic	false
C37	CB	SER- 106	3.82	0	Hydrophobic	false
C32	CG	ARG- 122	4.2	0	Hydrophobic	false
C14	CD	ARG- 122	4.11	0	Hydrophobic	false
C21	CD	ARG- 122	4.18	0	Hydrophobic	false
O12	OD1	ASN- 123	3.34	132.17	H-Bond (Ligand Donor)	false
C8	CG2	VAL- 126	4.18	0	Hydrophobic	false
C32	CG2	VAL- 126	3.95	0	Hydrophobic	false
O11	NE2	HIS- 147	3.12	142.83	H-Bond (Protein Donor)	false
C34	CG2	ILE- 150	3.74	0	Hydrophobic	false
C33	CG2	ILE- 150	4.23	0	Hydrophobic	false
C34	CB	ALA- 151	3.76	0	Hydrophobic	false
C35	CG2	THR- 154	3.97	0	Hydrophobic	false
C12	CE	MET- 155	3.63	0	Hydrophobic	false
C36	SD	MET- 155	3.85	0	Hydrophobic	false