scPDB - 3sxn entry

Protein Data Bank Entry:

PDB ID : 3sxn

Resolution :2.030 Å

Experimental Method : X-ray

Deposition Date : 2011-07-15

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	N-acetyltransferase Eis
ID:	A0QY29_MYCS2
AC:	A0QY29
Organism:	Mycobacterium smegmatis 155)
Reign:	Bacteria
TaxID:	246196
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	9 %
C	91 %

Ligand binding site composition:

B-Factor:	24.656
Number of residues:	37
Including
Standard Amino Acids:	34
Non Standard Amino Acids:	0
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.410	756.000

% Hydrophobic	% Polar
41.96	58.04
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	60.44 %
Polar Surface area:	426.11 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	6
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
42.5964	-12.4773	56.6296

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
C6P	CE2	PHE- 26	4.33	0	Hydrophobic	false
C2P	CZ	PHE- 26	4.13	0	Hydrophobic	false
CEP	CG1	VAL- 85	4.14	0	Hydrophobic	false
C2P	CB	VAL- 85	3.67	0	Hydrophobic	false
CCP	CG2	VAL- 87	4.48	0	Hydrophobic	false
CEP	CG2	VAL- 87	3.78	0	Hydrophobic	false
CAP	CB	VAL- 87	4.33	0	Hydrophobic	false
O9P	N	VAL- 87	2.76	177.37	H-Bond (Protein Donor)	false
C2B	CD	ARG- 93	4.11	0	Hydrophobic	false
O4A	NH1	ARG- 93	2.93	139.39	H-Bond (Protein Donor)	false
O4A	N	ARG- 93	2.68	170.55	H-Bond (Protein Donor)	false
OAP	NH1	ARG- 93	3.02	151.81	H-Bond (Protein Donor)	false
O4A	CZ	ARG- 93	3.96	0	Ionic (Protein Cationic)	false
DuAr	CZ	ARG- 93	3.3	26	Pi/Cation	false
O2A	N	GLY- 95	3.01	141.45	H-Bond (Protein Donor)	false
O5A	N	LEU- 97	2.99	165.13	H-Bond (Protein Donor)	false
CCP	CD2	LEU- 97	3.95	0	Hydrophobic	false
CDP	CD2	LEU- 97	4.38	0	Hydrophobic	false
CEP	CD2	LEU- 97	4.41	0	Hydrophobic	false
O7A	NH1	ARG- 98	3.38	149.61	H-Bond (Protein Donor)	false
O1A	N	ARG- 98	2.99	148.67	H-Bond (Protein Donor)	false
C6P	CB	SER- 121	4.19	0	Hydrophobic	false
S1P	CB	SER- 121	3.99	0	Hydrophobic	false
N6A	OE2	GLU- 122	3.04	126.58	H-Bond (Ligand Donor)	false
CDP	CD1	ILE- 125	4.18	0	Hydrophobic	false
C2P	CZ	TYR- 126	4.35	0	Hydrophobic	false
S1P	CE2	TYR- 126	3.78	0	Hydrophobic	false
C1B	CD	ARG- 128	4.14	0	Hydrophobic	false
C4B	CD	ARG- 128	3.59	0	Hydrophobic	false
C5B	CZ	PHE- 129	4.46	0	Hydrophobic	false
OAP	OD2	ASP- 258	2.8	162.62	H-Bond (Ligand Donor)	false
C6P	CD1	LEU- 259	3.96	0	Hydrophobic	false
O5A	O	HOH- 816	2.63	148.39	H-Bond (Protein Donor)	false