scPDB - 3d91 entry

Protein Data Bank Entry:

PDB ID : 3d91

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2008-05-26

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	9.160	9.160	9.160	0.000	9.160	1

List of CHEMBLId :

CHEMBL31601

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
B	100 %

Ligand binding site composition:

B-Factor:	65.349
Number of residues:	40
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.347	1269.000

% Hydrophobic	% Polar
38.83	61.17
According to VolSite

Ligand :

HET Code:	REM
Formula:	C33H50N4O6S
Molecular weight:	630.838 g/mol
DrugBank ID:	DB00212
Buried Surface Area:	61.87 %
Polar Surface area:	169.85 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	5
Rings:	4
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	16

Mass center Coordinates

X	Y	Z
2.35773	-16.5974	9.77952

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
C43	CB	THR- 18	4.38	0	Hydrophobic	false
C6	CG	GLN- 19	4.19	0	Hydrophobic	false
C29	CG1	VAL- 36	3.81	0	Hydrophobic	false
O25	OD1	ASP- 38	2.78	174.95	H-Bond (Ligand Donor)	false
C27	CB	ASP- 38	4.1	0	Hydrophobic	false
C22	CD1	TYR- 83	4.28	0	Hydrophobic	false
C33	CG	TYR- 83	3.82	0	Hydrophobic	false
C32	CD2	TYR- 83	4.31	0	Hydrophobic	false
C28	CD1	TYR- 83	4.05	0	Hydrophobic	false
C15	CB	SER- 84	3.81	0	Hydrophobic	false
N17	OG	SER- 84	2.86	164.93	H-Bond (Protein Donor)	false
O26	N	SER- 84	3.09	155.16	H-Bond (Protein Donor)	false
O26	OG	SER- 84	2.52	157.65	H-Bond (Ligand Donor)	false
C1	CG2	THR- 85	4.24	0	Hydrophobic	false
C15	CG2	THR- 85	4.08	0	Hydrophobic	false
N11	OG1	THR- 85	3.4	173.77	H-Bond (Ligand Donor)	false
O14	N	THR- 85	3.35	160.08	H-Bond (Protein Donor)	false
C9	CB	PRO- 118	3.92	0	Hydrophobic	false
C32	CE1	PHE- 119	3.96	0	Hydrophobic	false
C10	CB	ALA- 122	4.04	0	Hydrophobic	false
C31	CZ	PHE- 124	3.85	0	Hydrophobic	false
C30	CG2	VAL- 127	3.55	0	Hydrophobic	false
C36	CD2	LEU- 224	3.82	0	Hydrophobic	false
C15	CB	ALA- 229	4.35	0	Hydrophobic	false
C43	CB	SER- 230	4.02	0	Hydrophobic	false
C37	CB	SER- 230	4.13	0	Hydrophobic	false
O3	N	SER- 230	2.94	168.24	H-Bond (Protein Donor)	false
C43	CZ	TYR- 231	4.17	0	Hydrophobic	false
C42	CE2	TYR- 231	3.71	0	Hydrophobic	false
N20	OG	SER- 233	2.52	144.54	H-Bond (Ligand Donor)	false
C15	SD	MET- 303	4.04	0	Hydrophobic	false