scPDB - 4h4q entry

Protein Data Bank Entry:

PDB ID : 4h4q

Resolution :1.950 Å

Experimental Method : X-ray

Deposition Date : 2012-09-18

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Biphenyl dioxygenase ferredoxin reductase subunit
ID:	E7FJB9_9BURK
AC:	E7FJB9
Organism:	Acidovorax sp. KKS102
Reign:	Bacteria
TaxID:	358220
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	13.228
Number of residues:	56
Including
Standard Amino Acids:	52
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.224	1096.875

% Hydrophobic	% Polar
46.46	53.54
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	74.12 %
Polar Surface area:	381.7 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
-34.1708	-12.9573	-9.42643

Binding mode :

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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'	CB	LEU- 17	4.25	0	Hydrophobic	false
O1P	N	ALA- 18	2.85	166.44	H-Bond (Protein Donor)	false
O2B	OD2	ASP- 40	2.65	160.86	H-Bond (Ligand Donor)	false
N3A	N	ASP- 40	3.13	131.37	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 41	2.93	136	H-Bond (Ligand Donor)	false
O2A	NH2	ARG- 48	3.34	132.23	H-Bond (Protein Donor)	false
O2A	NE	ARG- 48	2.77	167.69	H-Bond (Protein Donor)	false
O2A	CZ	ARG- 48	3.49	0	Ionic (Protein Cationic)	false
C1'	CB	ARG- 48	4.33	0	Hydrophobic	false
C9	CB	ARG- 48	3.6	0	Hydrophobic	false
C9A	CG	PRO- 49	4.33	0	Hydrophobic	false
C1'	CG	PRO- 49	3.64	0	Hydrophobic	false
C7M	CB	LEU- 51	4.15	0	Hydrophobic	false
C6	CB	SER- 52	4.26	0	Hydrophobic	false
C7M	CB	SER- 52	4.04	0	Hydrophobic	false
N6A	O	ALA- 82	2.93	163.03	H-Bond (Ligand Donor)	false
N1A	N	ALA- 82	3.11	159.55	H-Bond (Protein Donor)	false
C7M	CG	LEU- 129	3.86	0	Hydrophobic	false
O1A	CZ	ARG- 130	3.74	0	Ionic (Protein Cationic)	false
O1A	NH2	ARG- 130	2.94	155.26	H-Bond (Protein Donor)	false
C8M	CD	ARG- 130	3.92	0	Hydrophobic	false
C7M	CG2	ILE- 156	3.72	0	Hydrophobic	false
C6	CD1	ILE- 156	3.36	0	Hydrophobic	false
O4	OE2	GLU- 159	2.58	150.71	H-Bond (Protein Donor)	false
O4'	OD1	ASP- 273	2.71	154.38	H-Bond (Ligand Donor)	false
O2P	N	ASP- 273	2.91	152.87	H-Bond (Protein Donor)	false
O2	N	TRP- 291	2.96	173.78	H-Bond (Protein Donor)	false
C1'	CB	TRP- 291	4.46	0	Hydrophobic	false
C5'	CB	ALA- 294	3.72	0	Hydrophobic	false
N3	O	TRP- 320	2.92	142.96	H-Bond (Ligand Donor)	false
O1P	O	HOH- 610	2.91	179.96	H-Bond (Protein Donor)	false
O2P	O	HOH- 619	2.55	179.96	H-Bond (Protein Donor)	false
O1A	O	HOH- 627	2.53	179.95	H-Bond (Protein Donor)	false