scPDB - 2ggq entry

Protein Data Bank Entry:

PDB ID : 2ggq

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2006-03-24

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Dual sugar-1-phosphate nucleotidylyltransferase
ID:	Q975F9_SULTO
AC:	Q975F9
Organism:	Sulfolobus tokodaii
Reign:	Archaea
TaxID:	273063
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	37.246
Number of residues:	36
Including
Standard Amino Acids:	32
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	IOD

Cavity properties

Ligandability	Volume (Å3)
0.781	1255.500

% Hydrophobic	% Polar
33.06	66.94
According to VolSite

Ligand :

HET Code:	TTP
Formula:	C10H13N2O14P3
Molecular weight:	478.137 g/mol
DrugBank ID:	DB02452
Buried Surface Area:	63.1 %
Polar Surface area:	279.44 Å2

Number of
H-Bond Acceptors:	14
H-Bond Donors:	2
Rings:	2
Aromatic rings:	0
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
1.13745	40.2579	12.5084

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
C5M	CB	LEU- 6	4.08	0	Hydrophobic	false
O4	N	ALA- 8	3.18	148.03	H-Bond (Protein Donor)	false
O2B	N	SER- 10	3.41	122.22	H-Bond (Protein Donor)	false
O2G	OG	SER- 10	2.63	153.89	H-Bond (Protein Donor)	false
O1B	N	GLY- 11	2.89	140.04	H-Bond (Protein Donor)	false
O2G	N	GLU- 12	3.04	138.97	H-Bond (Protein Donor)	false
O3A	NH2	ARG- 13	2.8	149.57	H-Bond (Protein Donor)	false
O1G	N	ARG- 13	3.1	164.76	H-Bond (Protein Donor)	false
O1G	NE	ARG- 13	3.14	145.55	H-Bond (Protein Donor)	false
O3G	NE	ARG- 13	3.19	135.48	H-Bond (Protein Donor)	false
O1G	CZ	ARG- 13	3.99	0	Ionic (Protein Cationic)	false
O3A	NZ	LYS- 23	3.36	138.11	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 23	2.67	135.8	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 23	2.67	0	Ionic (Protein Cationic)	false
O2	NE2	GLN- 73	2.91	165	H-Bond (Protein Donor)	false
N3	OE1	GLN- 73	2.88	169.19	H-Bond (Ligand Donor)	false
O2	N	GLY- 79	3	166.62	H-Bond (Protein Donor)	false
C5M	CG2	THR- 80	4.2	0	Hydrophobic	false
O3'	OE1	GLU- 181	2.76	154.03	H-Bond (Ligand Donor)	false
C2'	CG	GLU- 181	4.22	0	Hydrophobic	false
O2G	NZ	LYS- 344	2.98	151.42	H-Bond (Protein Donor)	false
O2G	NZ	LYS- 344	2.98	0	Ionic (Protein Cationic)	false
O3G	NZ	LYS- 344	3.11	0	Ionic (Protein Cationic)	false
O1G	O	HOH- 622	2.7	144.25	H-Bond (Protein Donor)	false