scPDB - 3own entry

Protein Data Bank Entry:

PDB ID : 3own

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2010-09-20

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	7.250	7.360	7.360	0.110	7.470	2

List of CHEMBLId :

CHEMBL1644464

Binding Site :

Uniprot Annotation

Name:	Renin
ID:	RENI_HUMAN
AC:	P00797
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	3.4.23.15

Chains:

Chain Name:	Percentage of Residues within binding site
A	100 %

Ligand binding site composition:

B-Factor:	16.906
Number of residues:	54
Including
Standard Amino Acids:	49
Non Standard Amino Acids:	1
Water Molecules:	4
Cofactors:
Metals:	NA

Cavity properties

Ligandability	Volume (Å3)
1.452	1130.625

% Hydrophobic	% Polar
44.78	55.22
According to VolSite

Ligand :

HET Code:	3OX
Formula:	C37H48N4O7S
Molecular weight:	692.865 g/mol
DrugBank ID:	-
Buried Surface Area:	61.12 %
Polar Surface area:	162.51 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	4
Rings:	4
Aromatic rings:	3
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	10

Mass center Coordinates

X	Y	Z
-10.3996	-27.3255	-35.1497

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
C49	CG	GLN- 16	3.99	0	Hydrophobic	false
O8	OD2	ASP- 35	3.13	149.45	H-Bond (Ligand Donor)	false
O8	OD1	ASP- 35	2.67	145.7	H-Bond (Ligand Donor)	false
N18	O	GLY- 37	2.91	172.49	H-Bond (Ligand Donor)	false
C17	CB	SER- 38	4.43	0	Hydrophobic	false
C3	CD1	TYR- 80	3.98	0	Hydrophobic	false
C7	CD1	TYR- 80	3.84	0	Hydrophobic	false
O12	N	SER- 81	3.01	134.93	H-Bond (Protein Donor)	false
C28	CG2	THR- 82	3.93	0	Hydrophobic	false
C20	CG2	THR- 82	3.7	0	Hydrophobic	false
O32	N	THR- 82	3.48	126.83	H-Bond (Protein Donor)	false
O32	OG1	THR- 82	2.77	126.42	H-Bond (Protein Donor)	false
C41	CG	PRO- 115	4.06	0	Hydrophobic	false
C46	CB	PRO- 115	3.56	0	Hydrophobic	false
C47	CB	LEU- 118	3.51	0	Hydrophobic	false
C39	CG2	VAL- 124	4.27	0	Hydrophobic	false
C43	CG2	VAL- 124	4.13	0	Hydrophobic	false
C17	CB	GLN- 132	3.89	0	Hydrophobic	false
C16	CD1	ILE- 134	4	0	Hydrophobic	false
C10	CG	LEU- 221	4.3	0	Hydrophobic	false
N1	O	GLY- 225	3.19	152.61	H-Bond (Ligand Donor)	false
C30	CB	ALA- 226	3.44	0	Hydrophobic	false
C21	CB	ALA- 226	4.04	0	Hydrophobic	false
O31	N	SER- 227	2.93	141.72	H-Bond (Protein Donor)	false
O31	OG	SER- 227	2.72	151.29	H-Bond (Protein Donor)	false
C30	CB	TYR- 228	3.34	0	Hydrophobic	false
C28	CB	HIS- 298	4.37	0	Hydrophobic	false
C10	CE	MET- 300	3.79	0	Hydrophobic	false
C20	SD	MET- 300	3.89	0	Hydrophobic	false
C28	SD	MET- 300	4.02	0	Hydrophobic	false
C11	CG1	ILE- 302	4.25	0	Hydrophobic	false