scPDB - 1bil entry

Protein Data Bank Entry:

PDB ID : 1bil

Resolution :2.400 Å

Experimental Method : X-ray

Deposition Date : 1995-09-27

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:	15.975
Number of residues:	42
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.399	1171.125

% Hydrophobic	% Polar
38.90	61.10
According to VolSite

Ligand :

HET Code:	0IU
Formula:	C34H53N5O5S
Molecular weight:	643.880 g/mol
DrugBank ID:	-
Buried Surface Area:	62.77 %
Polar Surface area:	177.33 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	4
Rings:	3
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	16

Mass center Coordinates

X	Y	Z
37.172	60.76	44.8507

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
C2'	CG1	VAL- 30	4.18	0	Hydrophobic	false
O11	OD1	ASP- 32	2.73	170.47	H-Bond (Ligand Donor)	false
C31	CD1	TYR- 75	3.57	0	Hydrophobic	false
C6'	CG	TYR- 75	3.79	0	Hydrophobic	false
C11	CD1	TYR- 75	3.98	0	Hydrophobic	false
CB1	CB	SER- 76	4.35	0	Hydrophobic	false
C12	CB	SER- 76	4.45	0	Hydrophobic	false
O12	N	SER- 76	3.19	161.52	H-Bond (Protein Donor)	false
CG2	CB	THR- 77	3.99	0	Hydrophobic	false
CB1	CG2	THR- 77	3.52	0	Hydrophobic	false
O2	OG1	THR- 77	3.11	164.79	H-Bond (Protein Donor)	false
CG2	CB	PRO- 111	4.47	0	Hydrophobic	false
CD1	CB	PRO- 111	3.23	0	Hydrophobic	false
C4'	CE1	PHE- 112	3.96	0	Hydrophobic	false
CE1	CB	LEU- 114	4.13	0	Hydrophobic	false
CZ	CB	ALA- 115	4.08	0	Hydrophobic	false
C3'	CZ	PHE- 117	3.42	0	Hydrophobic	false
C4'	CE2	PHE- 117	3.61	0	Hydrophobic	false
C4'	CG2	VAL- 120	3.91	0	Hydrophobic	false
C41	CD2	LEU- 213	4.26	0	Hydrophobic	false
C5	CD2	LEU- 213	3.84	0	Hydrophobic	false
N2	O	GLY- 217	2.73	150.65	H-Bond (Ligand Donor)	false
CA1	CB	ALA- 218	4.18	0	Hydrophobic	false
SE2	CB	ALA- 218	4.24	0	Hydrophobic	false
O1	N	SER- 219	3.15	169.41	H-Bond (Protein Donor)	false
NZ	O	TYR- 220	3.04	146.85	H-Bond (Ligand Donor)	false
SE2	CB	SER- 222	4.34	0	Hydrophobic	false
NZ	OG	SER- 222	3.07	121.63	H-Bond (Ligand Donor)	false
CB1	CE	MET- 289	3.77	0	Hydrophobic	false
SE2	CG	MET- 289	4.09	0	Hydrophobic	false
SE2	CD1	ILE- 291	4.46	0	Hydrophobic	false
C5	CD1	ILE- 291	3.75	0	Hydrophobic	false
SE2	CB	ALA- 300	3.84	0	Hydrophobic	false
ND1	O	HOH- 803	2.63	179.97	H-Bond (Protein Donor)	false