scPDB - 1tiq entry

Protein Data Bank Entry:

PDB ID : 1tiq

Resolution :1.900 Å

Experimental Method : X-ray

Deposition Date : 2004-06-02

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Spermidine/spermine N(1)-acetyltransferase
ID:	PAIA_BACSU
AC:	P21340
Organism:	Bacillus subtilis
Reign:	Bacteria
TaxID:	224308
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	13.745
Number of residues:	51
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	0
Water Molecules:	6
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.924	995.625

% Hydrophobic	% Polar
43.39	56.61
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	58.23 %
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
16.574	66.3835	60.512

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
CDP	CZ	PHE- 24	3.99	0	Hydrophobic	false
CEP	CE2	PHE- 24	4.02	0	Hydrophobic	false
C6P	CG2	THR- 27	4.05	0	Hydrophobic	false
CEP	CZ	PHE- 28	4.22	0	Hydrophobic	false
O3A	OH	TYR- 40	3	160.96	H-Bond (Protein Donor)	false
O6A	OH	TYR- 40	3.49	138.45	H-Bond (Protein Donor)	false
CDP	CE2	TYR- 40	3.5	0	Hydrophobic	false
CDP	CG1	ILE- 96	3.97	0	Hydrophobic	false
N4P	O	ILE- 96	2.84	137.08	H-Bond (Ligand Donor)	false
C6P	CD1	TYR- 97	3.63	0	Hydrophobic	false
S1P	CZ	TYR- 97	3.67	0	Hydrophobic	false
S1P	CE2	TYR- 97	3.63	0	Hydrophobic	false
CDP	CG1	ILE- 98	4.01	0	Hydrophobic	false
CAP	CB	ILE- 98	4.13	0	Hydrophobic	false
O9P	N	ILE- 98	2.74	151.58	H-Bond (Protein Donor)	false
CAP	CG	GLN- 103	3.86	0	Hydrophobic	false
O4A	N	LYS- 104	3.4	140.18	H-Bond (Protein Donor)	false
O5A	N	LYS- 104	3.2	162.1	H-Bond (Protein Donor)	false
O2A	N	GLY- 106	2.85	152.74	H-Bond (Protein Donor)	false
O4A	N	GLY- 108	3.33	146.27	H-Bond (Protein Donor)	false
O7A	NZ	LYS- 109	3.43	131.53	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 109	2.79	166.22	H-Bond (Protein Donor)	false
O1A	N	LYS- 109	2.94	157.16	H-Bond (Protein Donor)	false
O7A	NZ	LYS- 109	3.43	0	Ionic (Protein Cationic)	false
O8A	NZ	LYS- 109	2.79	0	Ionic (Protein Cationic)	false
C5B	CB	LYS- 109	4.07	0	Hydrophobic	false
O5P	N	TRP- 132	2.91	155.05	H-Bond (Protein Donor)	false
O5P	ND2	ASN- 135	2.73	160.77	H-Bond (Protein Donor)	false
N6A	OD1	ASN- 137	2.77	153.4	H-Bond (Ligand Donor)	false
OAP	ND2	ASN- 137	3.05	136.01	H-Bond (Protein Donor)	false
CEP	CB	ALA- 138	4.28	0	Hydrophobic	false
C2P	CB	ALA- 138	4.17	0	Hydrophobic	false
C5B	CE2	PHE- 141	4.45	0	Hydrophobic	false
CCP	CZ	PHE- 141	3.81	0	Hydrophobic	false
CDP	CE1	PHE- 141	4.32	0	Hydrophobic	false
CEP	CD1	PHE- 141	3.85	0	Hydrophobic	false
C2P	CZ	TYR- 142	4.48	0	Hydrophobic	false
C1B	CG	LYS- 144	4.18	0	Hydrophobic	false
O3B	NZ	LYS- 144	3.42	125.54	H-Bond (Protein Donor)	false
O9A	NZ	LYS- 144	3.45	0	Ionic (Protein Cationic)	false
C4B	CE	MET- 145	3.74	0	Hydrophobic	false
CAP	CE2	PHE- 155	3.65	0	Hydrophobic	false
O5P	O	HOH- 1205	2.72	179.96	H-Bond (Protein Donor)	false
O4A	O	HOH- 1312	2.61	158.35	H-Bond (Protein Donor)	false
N4P	O	HOH- 1319	3.3	126.36	H-Bond (Ligand Donor)	false