scPDB - 2onf entry

Protein Data Bank Entry:

PDB ID : 2onf

Resolution :1.700 Å

Experimental Method : X-ray

Deposition Date : 2007-01-23

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Uncharacterized protein
ID:	Q9HLN2_THEAC
AC:	Q9HLN2
Organism:	Thermoplasma acidophilum
Reign:	Archaea
TaxID:	273075
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	43 %
B	57 %

Ligand binding site composition:

B-Factor:	21.510
Number of residues:	35
Including
Standard Amino Acids:	30
Non Standard Amino Acids:	0
Water Molecules:	5
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.220	307.125

% Hydrophobic	% Polar
53.85	46.15
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	51.34 %
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
3.34802	8.79356	5.65644

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
S1P	CB	SER- 29	4.26	0	Hydrophobic	false
C2P	CD2	PHE- 33	3.71	0	Hydrophobic	false
S1P	CG	PRO- 42	4.38	0	Hydrophobic	false
S1P	CB	THR- 56	4.22	0	Hydrophobic	false
CEP	CG	GLU- 60	3.94	0	Hydrophobic	false
C6P	CG	GLU- 60	3.93	0	Hydrophobic	false
C1B	CE1	PHE- 61	4.28	0	Hydrophobic	false
CDP	CZ	PHE- 61	3.98	0	Hydrophobic	false
CEP	CZ	PHE- 61	3.91	0	Hydrophobic	false
N7A	NH1	ARG- 64	3.03	150.95	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 86	2.66	171.04	H-Bond (Protein Donor)	false
O2A	NZ	LYS- 86	2.88	167.8	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 86	2.66	0	Ionic (Protein Cationic)	false
O2A	NZ	LYS- 86	2.88	0	Ionic (Protein Cationic)	false
O5A	N	GLY- 87	3.05	160.53	H-Bond (Protein Donor)	false
CAP	CE2	PHE- 88	4.06	0	Hydrophobic	false
O7A	CZ	ARG- 111	3.65	0	Ionic (Protein Cationic)	false
O7A	NH1	ARG- 111	3.37	139.82	H-Bond (Protein Donor)	false
O7A	NH2	ARG- 111	3.01	159.43	H-Bond (Protein Donor)	false
C1B	CD1	LEU- 115	3.9	0	Hydrophobic	false
C4B	CD2	LEU- 115	3.82	0	Hydrophobic	false
O9A	NZ	LYS- 118	2.79	165.01	H-Bond (Protein Donor)	false
O9A	NZ	LYS- 118	2.79	0	Ionic (Protein Cationic)	false
O9A	OH	TYR- 119	2.56	168.68	H-Bond (Protein Donor)	false
C4B	CE2	TYR- 119	3.6	0	Hydrophobic	false
C5B	CZ	TYR- 119	3.45	0	Hydrophobic	false
CDP	CD1	TYR- 119	3.49	0	Hydrophobic	false
C2P	CE2	PHE- 121	3.72	0	Hydrophobic	false
O9P	O	HOH- 147	2.74	167.59	H-Bond (Protein Donor)	false
O5P	O	HOH- 155	2.69	154.63	H-Bond (Protein Donor)	false
N4P	O	HOH- 168	3.41	131.09	H-Bond (Ligand Donor)	false
N3A	O	HOH- 171	2.73	179.94	H-Bond (Protein Donor)	false
O7A	O	HOH- 222	2.73	179.95	H-Bond (Protein Donor)	false