scPDB - 1kux entry

Protein Data Bank Entry:

PDB ID : 1kux

Resolution :1.800 Å

Experimental Method : X-ray

Deposition Date : 2002-01-22

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Serotonin N-acetyltransferase
ID:	SNAT_SHEEP
AC:	Q29495
Organism:	Ovis aries
Reign:	Eukaryota
TaxID:	9940
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	13.418
Number of residues:	45
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.236	826.875

% Hydrophobic	% Polar
53.88	46.12
According to VolSite

Ligand :

HET Code:	CA3
Formula:	C36H50N9O17P3S
Molecular weight:	1005.819 g/mol
DrugBank ID:	DB01777
Buried Surface Area:	56.43 %
Polar Surface area:	457.5 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	5
Aromatic rings:	4
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	27

Mass center Coordinates

X	Y	Z
17.473	24.5945	30.5032

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
CP4	CB	ALA- 55	3.75	0	Hydrophobic	false
CP4	CZ	PHE- 56	3.7	0	Hydrophobic	false
CT8	CB	ASN- 62	4.17	0	Hydrophobic	false
C11	CB	PRO- 64	3.65	0	Hydrophobic	false
CA5	CB	LEU- 121	4.1	0	Hydrophobic	false
CPA	CG	LEU- 124	4.23	0	Hydrophobic	false
CA5	CB	LEU- 124	4	0	Hydrophobic	false
NP1	O	LEU- 124	2.75	152.48	H-Bond (Ligand Donor)	false
OA2	N	LEU- 124	2.85	138.09	H-Bond (Protein Donor)	false
CP4	CB	ALA- 125	4.07	0	Hydrophobic	false
CPA	CG2	VAL- 126	4.12	0	Hydrophobic	false
OP2	N	VAL- 126	2.85	169.69	H-Bond (Protein Donor)	false
CP7	CD	ARG- 131	4.1	0	Hydrophobic	false
OP2	NE	ARG- 131	3.32	131.46	H-Bond (Protein Donor)	false
O22	N	GLN- 132	2.75	169.61	H-Bond (Protein Donor)	false
O12	N	GLY- 134	2.88	147.48	H-Bond (Protein Donor)	false
O21	N	GLY- 136	2.71	152.59	H-Bond (Protein Donor)	false
O11	OG	SER- 137	2.79	153.4	H-Bond (Protein Donor)	false
O11	N	SER- 137	3.02	145.95	H-Bond (Protein Donor)	false
CA4	CB	LEU- 158	3.74	0	Hydrophobic	false
CT2	CE	MET- 159	4.15	0	Hydrophobic	false
C11	CE	MET- 159	3.95	0	Hydrophobic	false
CA1	CB	CYS- 160	3.54	0	Hydrophobic	false
C1'	CD2	LEU- 164	3.8	0	Hydrophobic	false
CPB	CD1	LEU- 164	4.47	0	Hydrophobic	false
S	CD1	LEU- 164	3.33	0	Hydrophobic	false
C4'	CD1	PHE- 167	3.68	0	Hydrophobic	false
C5'	CE1	PHE- 167	4.11	0	Hydrophobic	false
CA3	CZ	TYR- 168	3.74	0	Hydrophobic	false
S	CE1	TYR- 168	3.81	0	Hydrophobic	false
O3'	NH2	ARG- 170	3.41	133.99	H-Bond (Protein Donor)	false
O32	NH1	ARG- 170	3.07	138.71	H-Bond (Protein Donor)	false
O32	NH2	ARG- 170	2.89	147.83	H-Bond (Protein Donor)	false
O33	NH2	ARG- 170	3.15	139.02	H-Bond (Protein Donor)	false
O32	CZ	ARG- 170	3.41	0	Ionic (Protein Cationic)	false
CT8	CG1	VAL- 183	3.45	0	Hydrophobic	false
CT7	CD1	LEU- 186	3.87	0	Hydrophobic	false
CT2	CE2	PHE- 188	3.94	0	Hydrophobic	false
NT1	O	HOH- 504	3.1	159.61	H-Bond (Ligand Donor)	false
O21	O	HOH- 508	2.65	159.8	H-Bond (Protein Donor)	false