scPDB - 1ib1 entry

Protein Data Bank Entry:

PDB ID : 1ib1

Resolution :2.700 Å

Experimental Method : X-ray

Deposition Date : 2001-03-26

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	7.320	7.320	7.320	0.000	7.320	1

List of CHEMBLId :

CHEMBL3144228

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
E	100 %

Ligand binding site composition:

B-Factor:	13.069
Number of residues:	42
Including
Standard Amino Acids:	42
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.685	631.125

% Hydrophobic	% Polar
47.59	52.41
According to VolSite

Ligand :

HET Code:	COT
Formula:	C33H44N9O17P3S
Molecular weight:	963.739 g/mol
DrugBank ID:	DB02931
Buried Surface Area:	58.08 %
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:	24

Mass center Coordinates

X	Y	Z
91.8587	44.47	62.4304

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
C6P	CB	ALA- 55	4.2	0	Hydrophobic	false
C6P	CE1	PHE- 56	3.53	0	Hydrophobic	false
C1P	CE1	PHE- 56	3.93	0	Hydrophobic	false
C16	CD1	PHE- 56	3.29	0	Hydrophobic	false
C17	CB	PHE- 56	3.97	0	Hydrophobic	false
C17	CB	SER- 60	4.46	0	Hydrophobic	false
C15	CB	ASN- 62	4.31	0	Hydrophobic	false
C1T	CG	PRO- 64	4.31	0	Hydrophobic	false
C11	CG	PRO- 64	3.7	0	Hydrophobic	false
C6T	CB	LEU- 124	4.3	0	Hydrophobic	false
CFP	CG	LEU- 124	4.05	0	Hydrophobic	false
O5T	N	LEU- 124	2.92	139.86	H-Bond (Protein Donor)	false
N3P	O	LEU- 124	2.86	149.7	H-Bond (Ligand Donor)	false
C6P	CB	ALA- 125	4.37	0	Hydrophobic	false
OAP	N	VAL- 126	2.62	159.19	H-Bond (Protein Donor)	false
CBP	CB	VAL- 126	4.04	0	Hydrophobic	false
CFP	CG2	VAL- 126	4.01	0	Hydrophobic	false
CBP	CD	ARG- 131	4.03	0	Hydrophobic	false
O13	N	GLN- 132	2.95	171.5	H-Bond (Protein Donor)	false
O15	N	GLY- 134	2.55	132.09	H-Bond (Protein Donor)	false
O12	N	GLY- 136	2.82	135.37	H-Bond (Protein Donor)	false
O16	N	SER- 137	2.92	141.51	H-Bond (Protein Donor)	false
O16	OG	SER- 137	2.51	157.75	H-Bond (Protein Donor)	false
C1T	CG	MET- 159	3.73	0	Hydrophobic	false
N3T	O	MET- 159	2.95	175.44	H-Bond (Ligand Donor)	false
S	CB	CYS- 160	3.48	0	Hydrophobic	false
CEP	CD2	LEU- 164	4.01	0	Hydrophobic	false
C1P	CD1	LEU- 164	3.71	0	Hydrophobic	false
CGP	CZ	PHE- 167	3.97	0	Hydrophobic	false
C4B	CE1	PHE- 167	3.6	0	Hydrophobic	false
C1B	CD1	PHE- 167	3.41	0	Hydrophobic	false
S	CE2	TYR- 168	3.73	0	Hydrophobic	false
C6T	CZ	TYR- 168	3.96	0	Hydrophobic	false
O3B	NH2	ARG- 170	2.88	154.87	H-Bond (Protein Donor)	false
C15	CD1	LEU- 186	4.19	0	Hydrophobic	false
C1T	CE1	PHE- 188	4.37	0	Hydrophobic	false