scPDB - 1eu1 entry

Protein Data Bank Entry:

PDB ID : 1eu1

Resolution :1.300 Å

Experimental Method : X-ray

Deposition Date : 2000-04-13

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Dimethyl sulfoxide/trimethylamine N-oxide reductase
ID:	DSTOR_RHOSH
AC:	Q57366
Organism:	Rhodobacter sphaeroides
Reign:	Bacteria
TaxID:	1063
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	10.135
Number of residues:	58
Including
Standard Amino Acids:	57
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.987	766.125

% Hydrophobic	% Polar
54.19	45.81
According to VolSite

Ligand :

HET Code:	MGD
Formula:	C20H24N10O13P2S2
Molecular weight:	738.541 g/mol
DrugBank ID:	-
Buried Surface Area:	79.93 %
Polar Surface area:	440.93 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	10
Rings:	6
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
22.2463	35.559	29.7791

Binding mode :

What is Poseview ?

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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
S13	CZ2	TRP- 116	3.53	0	Hydrophobic	false
S12	CB	SER- 147	3.71	0	Hydrophobic	false
O1B	NZ	LYS- 190	2.77	167.25	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 190	2.77	0	Ionic (Protein Cationic)	false
N22	O	THR- 191	2.96	155.7	H-Bond (Ligand Donor)	false
C23	CB	THR- 191	4.01	0	Hydrophobic	false
C10	CG2	THR- 191	3.99	0	Hydrophobic	false
N19	OE2	GLU- 193	3.48	126.15	H-Bond (Ligand Donor)	false
N2	O	ILE- 220	3.04	167.71	H-Bond (Ligand Donor)	false
O3'	ND2	ASN- 221	2.93	171.01	H-Bond (Protein Donor)	false
O2'	OD1	ASN- 221	2.72	163.82	H-Bond (Ligand Donor)	false
O6	N	GLN- 241	2.98	154.45	H-Bond (Protein Donor)	false
N1	OD2	ASP- 243	2.81	149.85	H-Bond (Ligand Donor)	false
N2	OD1	ASP- 243	2.86	151.06	H-Bond (Ligand Donor)	false
O2A	N	TRP- 322	2.99	177.86	H-Bond (Protein Donor)	false
S12	CE3	TRP- 322	3.45	0	Hydrophobic	false
C5'	CB	SER- 323	4.14	0	Hydrophobic	false
O4'	OG	SER- 323	2.89	171.82	H-Bond (Protein Donor)	false
O2B	NH1	ARG- 326	3.3	129.78	H-Bond (Protein Donor)	false
O1A	NH2	ARG- 326	2.81	148.36	H-Bond (Protein Donor)	false
O1A	NH1	ARG- 326	2.95	140.27	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 326	3.32	0	Ionic (Protein Cationic)	false
C2'	CG1	VAL- 640	4.21	0	Hydrophobic	false
C2'	CB	SER- 642	4.44	0	Hydrophobic	false
O1B	N	HIS- 643	3.12	163.76	H-Bond (Protein Donor)	false
C10	CB	HIS- 643	4.4	0	Hydrophobic	false
N18	O	ARG- 647	2.97	139.86	H-Bond (Ligand Donor)	false
O17	N	HIS- 649	2.94	150.05	H-Bond (Protein Donor)	false
O2B	NE2	GLN- 755	3	146.14	H-Bond (Protein Donor)	false