scPDB - 2wow entry

Protein Data Bank Entry:

PDB ID : 2wow

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2009-07-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Trypanothione reductase
ID:	Q389T8_TRYB2
AC:	Q389T8
Organism:	Trypanosoma brucei brucei
Reign:	Eukaryota
TaxID:	185431
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	5 %
B	95 %

Ligand binding site composition:

B-Factor:	20.592
Number of residues:	43
Including
Standard Amino Acids:	40
Non Standard Amino Acids:	1
Water Molecules:	2
Cofactors:	FAD
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.683	712.125

% Hydrophobic	% Polar
46.45	53.55
According to VolSite

Ligand :

HET Code:	NDP
Formula:	C21H26N7O17P3
Molecular weight:	741.389 g/mol
DrugBank ID:	DB02338
Buried Surface Area:	62.18 %
Polar Surface area:	404.9 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	5
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
14.5554	-4.83029	100.59

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
O3B	N	GLY- 196	2.88	141.42	H-Bond (Protein Donor)	false
C3D	CD2	PHE- 198	3.48	0	Hydrophobic	false
C5N	CB	PHE- 198	3.39	0	Hydrophobic	false
O1N	N	ILE- 199	2.86	159.98	H-Bond (Protein Donor)	false
C5D	CD1	ILE- 199	4.45	0	Hydrophobic	false
C5N	CG1	ILE- 199	3.44	0	Hydrophobic	false
N7N	OE2	GLU- 202	3.09	142.83	H-Bond (Ligand Donor)	false
O1X	OH	TYR- 221	3.16	150.48	H-Bond (Protein Donor)	false
O2X	OH	TYR- 221	3.1	140.2	H-Bond (Protein Donor)	false
C2B	CE1	TYR- 221	4.31	0	Hydrophobic	false
O2X	NH2	ARG- 222	3.33	136.98	H-Bond (Protein Donor)	false
O2X	NE	ARG- 222	3.13	147.34	H-Bond (Protein Donor)	false
O3X	NH2	ARG- 222	3.14	155.78	H-Bond (Protein Donor)	false
O2X	CZ	ARG- 222	3.67	0	Ionic (Protein Cationic)	false
DuAr	CZ	ARG- 222	3.95	157.18	Pi/Cation	false
O1X	CZ	ARG- 228	3.55	0	Ionic (Protein Cationic)	false
O3X	CZ	ARG- 228	3.81	0	Ionic (Protein Cationic)	false
O1X	NE	ARG- 228	2.76	175.95	H-Bond (Protein Donor)	false
O1X	NH2	ARG- 228	3.48	128.64	H-Bond (Protein Donor)	false
O3X	NH2	ARG- 228	2.92	158.01	H-Bond (Protein Donor)	false
C1B	CB	ILE- 285	4.49	0	Hydrophobic	false
O2N	N	GLY- 286	3.11	133.9	H-Bond (Protein Donor)	false
C5D	CD	ARG- 287	3.91	0	Hydrophobic	false
C4D	CB	MET- 333	4.46	0	Hydrophobic	false
O2D	O	MET- 333	2.91	163.51	H-Bond (Ligand Donor)	false
O1N	O	HOH- 2095	2.66	169.31	H-Bond (Protein Donor)	false