scPDB - 3h1j entry

Protein Data Bank Entry:

PDB ID : 3h1j

Resolution :3.000 Å

Experimental Method : X-ray

Deposition Date : 2009-04-12

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Cytochrome b
ID:	CYB_CHICK
AC:	P18946
Organism:	Gallus gallus
Reign:	Eukaryota
TaxID:	9031
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
P	89 %
E	11 %

Ligand binding site composition:

B-Factor:	72.685
Number of residues:	46
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.977	766.125

% Hydrophobic	% Polar
76.21	23.79
According to VolSite

Ligand :

HET Code:	SMA
Formula:	C30H42O7
Molecular weight:	514.650 g/mol
DrugBank ID:	-
Buried Surface Area:	64.72 %
Polar Surface area:	83.45 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	1
Rings:	2
Aromatic rings:	1
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
50.7105	143.823	86.703

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
C25	CD2	LEU- 122	3.9	0	Hydrophobic	false
C12	SD	MET- 125	4.27	0	Hydrophobic	false
C22	SD	MET- 125	4.04	0	Hydrophobic	false
C23	SD	MET- 125	4.29	0	Hydrophobic	false
C25	CB	MET- 125	3.98	0	Hydrophobic	false
C24	CB	PHE- 129	3.99	0	Hydrophobic	false
C26	CE2	PHE- 129	4.07	0	Hydrophobic	false
C21	CG1	VAL- 130	4.37	0	Hydrophobic	false
C7M	CE2	TYR- 132	4.33	0	Hydrophobic	false
C7M	SD	MET- 139	4.44	0	Hydrophobic	false
C5M	CG2	VAL- 146	3.56	0	Hydrophobic	false
C6	CG2	VAL- 146	4.49	0	Hydrophobic	false
C5	CG1	VAL- 146	3.83	0	Hydrophobic	false
C8	CD1	ILE- 147	4.22	0	Hydrophobic	false
C13	CG2	ILE- 147	4.19	0	Hydrophobic	false
C24	CD1	ILE- 147	4.12	0	Hydrophobic	false
C26	CG2	THR- 148	3.7	0	Hydrophobic	false
C26	CE1	PHE- 151	3.77	0	Hydrophobic	false
C5M	CB	CYS- 160	3.55	0	Hydrophobic	false
O4	NE2	HIS- 161	2.98	170.43	H-Bond (Protein Donor)	false
O5	NE2	HIS- 161	3.27	122.57	H-Bond (Protein Donor)	false
C21	CE1	PHE- 179	3.61	0	Hydrophobic	false
C21	CD2	LEU- 182	3.74	0	Hydrophobic	false
C5M	CD1	ILE- 269	4.26	0	Hydrophobic	false
C6	CD1	ILE- 269	4.32	0	Hydrophobic	false
C7M	CB	PRO- 271	4.35	0	Hydrophobic	false
C8	CB	PRO- 271	3.47	0	Hydrophobic	false
C4A	CG	PRO- 271	3.43	0	Hydrophobic	false
C22	CD1	PHE- 275	3.65	0	Hydrophobic	false
C24	CZ	PHE- 275	3.69	0	Hydrophobic	false
C9	CD2	PHE- 275	3.51	0	Hydrophobic	false
C22	CB	ALA- 278	3.8	0	Hydrophobic	false
C3M	CD1	TYR- 279	4.34	0	Hydrophobic	false
C5M	CE1	TYR- 279	4.3	0	Hydrophobic	false
C3M	CD1	LEU- 282	4.09	0	Hydrophobic	false
C3M	CD2	LEU- 295	3.52	0	Hydrophobic	false
C10	CD2	LEU- 295	4.14	0	Hydrophobic	false
C22	CD1	LEU- 295	4.42	0	Hydrophobic	false
C23	CD1	LEU- 295	3.79	0	Hydrophobic	false
C23	CG2	VAL- 299	4.47	0	Hydrophobic	false