scPDB - 1lqu entry

Protein Data Bank Entry:

PDB ID : 1lqu

Resolution :1.250 Å

Experimental Method : X-ray

Deposition Date : 2002-05-13

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	NADPH-ferredoxin reductase FprA
ID:	FPRA_MYCTU
AC:	P9WIQ3
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	1.18.1.2

Chains:

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

Ligand binding site composition:

B-Factor:	9.723
Number of residues:	63
Including
Standard Amino Acids:	55
Non Standard Amino Acids:	1
Water Molecules:	7
Cofactors:	NDP
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.603	857.250

% Hydrophobic	% Polar
62.99	37.01
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	77.24 %
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
3.17004	-10.5553	15.3941

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
C4'	CG	PRO- 13	3.9	0	Hydrophobic	false
O1P	N	SER- 14	2.97	150.82	H-Bond (Protein Donor)	false
O1P	OG	SER- 14	2.72	159.01	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 40	2.65	166.13	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 40	2.66	168.58	H-Bond (Ligand Donor)	false
C2B	CE	MET- 41	4.13	0	Hydrophobic	false
N3A	N	MET- 41	3.03	139.56	H-Bond (Protein Donor)	false
O2A	N	LEU- 48	2.95	171.31	H-Bond (Protein Donor)	false
C8M	CD1	LEU- 48	3.76	0	Hydrophobic	false
N6A	O	VAL- 84	2.95	164.97	H-Bond (Ligand Donor)	false
N1A	N	VAL- 84	3.09	158.35	H-Bond (Protein Donor)	false
C7M	CG1	VAL- 129	3.83	0	Hydrophobic	false
C7	CG2	VAL- 158	3.78	0	Hydrophobic	false
C7M	CZ	TYR- 324	4.21	0	Hydrophobic	false
C8M	CZ	TYR- 324	3.41	0	Hydrophobic	false
C8M	CH2	TRP- 359	3.88	0	Hydrophobic	false
C3'	CZ2	TRP- 359	3.55	0	Hydrophobic	false
C5'	CE2	TRP- 359	3.9	0	Hydrophobic	false
O2P	N	TRP- 359	2.83	166.21	H-Bond (Protein Donor)	false
O3'	O	GLY- 366	2.8	143.21	H-Bond (Ligand Donor)	false
N1	N	ILE- 368	3.39	129.51	H-Bond (Protein Donor)	false
O2	N	ILE- 368	2.9	172.25	H-Bond (Protein Donor)	false
C2'	CG1	ILE- 368	3.93	0	Hydrophobic	false
O3'	ND2	ASN- 371	3.03	146.38	H-Bond (Protein Donor)	false
N5	O	HOH- 1461	3.06	161.75	H-Bond (Protein Donor)	false
O2P	O	HOH- 1465	2.81	169.9	H-Bond (Protein Donor)	false
O1P	O	HOH- 1467	2.72	152.75	H-Bond (Protein Donor)	false
O2B	O	HOH- 1469	2.8	179.95	H-Bond (Protein Donor)	false
O3B	O	HOH- 1486	2.85	133.44	H-Bond (Protein Donor)	false