scPDB - 2g20 entry

Protein Data Bank Entry:

PDB ID : 2g20

Resolution :2.400 Å

Experimental Method : X-ray

Deposition Date : 2006-02-15

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

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:	34.536
Number of residues:	44
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.379	1326.375

% Hydrophobic	% Polar
44.78	55.22
According to VolSite

Ligand :

HET Code:	L1A
Formula:	C33H50N6O7S2
Molecular weight:	706.916 g/mol
DrugBank ID:	-
Buried Surface Area:	63.55 %
Polar Surface area:	232.82 Å2

Number of
H-Bond Acceptors:	9
H-Bond Donors:	6
Rings:	4
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	17

Mass center Coordinates

X	Y	Z
10.5789	44.2804	104.374

Binding mode :

What is Poseview ?

2D View
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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
C5	CG	GLN- 14	3.93	0	Hydrophobic	false
C28	CG1	VAL- 31	4.37	0	Hydrophobic	false
C33	CG2	VAL- 31	3.96	0	Hydrophobic	false
O3	OD2	ASP- 33	3	149.79	H-Bond (Ligand Donor)	false
C30	CB	TYR- 78	3.94	0	Hydrophobic	false
C17	CG	TYR- 78	3.5	0	Hydrophobic	false
C18	CD2	TYR- 78	4.39	0	Hydrophobic	false
C13	CB	SER- 79	3.99	0	Hydrophobic	false
C19	CB	SER- 79	4.46	0	Hydrophobic	false
C22	CB	SER- 79	4.29	0	Hydrophobic	false
O4	N	SER- 79	3.31	159.62	H-Bond (Protein Donor)	false
N1	OG1	THR- 80	2.93	153.76	H-Bond (Ligand Donor)	false
C13	CG2	THR- 80	3.72	0	Hydrophobic	false
C26	CG2	THR- 80	3.44	0	Hydrophobic	false
C3	CG	PRO- 113	4.33	0	Hydrophobic	false
C24	CB	PRO- 113	3.95	0	Hydrophobic	false
C27	CB	PRO- 113	4.23	0	Hydrophobic	false
C2	CB	PRO- 113	3.75	0	Hydrophobic	false
C31	CE2	PHE- 114	3.89	0	Hydrophobic	false
C24	CD1	LEU- 116	3.56	0	Hydrophobic	false
C1	CB	LEU- 116	4.05	0	Hydrophobic	false
C1	CB	ALA- 117	3.7	0	Hydrophobic	false
C32	CE2	PHE- 119	3.61	0	Hydrophobic	false
C33	CZ	PHE- 119	3.91	0	Hydrophobic	false
C32	CG2	VAL- 122	3.83	0	Hydrophobic	false
C22	CD2	LEU- 219	4.14	0	Hydrophobic	false
C23	CD2	LEU- 219	3.96	0	Hydrophobic	false
O3	OD2	ASP- 221	2.87	120.96	H-Bond (Ligand Donor)	false
N3	O	GLY- 223	2.73	148.27	H-Bond (Ligand Donor)	false
O1	N	SER- 225	2.82	160.52	H-Bond (Protein Donor)	false
N2	OG	SER- 225	3.04	151.71	H-Bond (Ligand Donor)	false
N4	O	TYR- 226	2.93	151.76	H-Bond (Ligand Donor)	false
S1	CB	SER- 228	4.27	0	Hydrophobic	false
C13	SD	MET- 298	4.12	0	Hydrophobic	false
S1	CG	MET- 298	3.57	0	Hydrophobic	false
S1	CD1	ILE- 300	4.07	0	Hydrophobic	false
C22	CD1	ILE- 300	3.66	0	Hydrophobic	false
C23	CG2	ILE- 300	4.21	0	Hydrophobic	false
S1	CB	ALA- 309	3.53	0	Hydrophobic	false