scPDB - 3gie entry

Protein Data Bank Entry:

PDB ID : 3gie

Resolution :2.650 Å

Experimental Method : X-ray

Deposition Date : 2009-03-05

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Sensor histidine kinase DesK
ID:	DESK_BACSU
AC:	O34757
Organism:	Bacillus subtilis
Reign:	Bacteria
TaxID:	224308
EC Number:	2.7.13.3

Chains:

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

Ligand binding site composition:

B-Factor:	99.999
Number of residues:	31
Including
Standard Amino Acids:	30
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
1.039	550.125

% Hydrophobic	% Polar
66.87	33.13
According to VolSite

Ligand :

HET Code:	ACP
Formula:	C11H14N5O12P3
Molecular weight:	501.176 g/mol
DrugBank ID:	DB03909
Buried Surface Area:	60.6 %
Polar Surface area:	310.64 Å2

Number of
H-Bond Acceptors:	16
H-Bond Donors:	3
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
31.0895	22.0791	28.3584

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
O3G	MG	MG- 1	2.05	0	Metal Acceptor	false
O2B	MG	MG- 1	2.05	0	Metal Acceptor	false
O1A	MG	MG- 1	2.06	0	Metal Acceptor	false
O1B	NE2	HIS- 297	3.4	149.62	H-Bond (Protein Donor)	false
C1'	CE1	PHE- 324	3.58	0	Hydrophobic	false
N3	N	LYS- 325	2.62	165.25	H-Bond (Protein Donor)	false
C2'	CB	LYS- 325	4.07	0	Hydrophobic	false
C4'	CB	SER- 330	3.38	0	Hydrophobic	false
O1G	OG	SER- 332	3.41	161.77	H-Bond (Protein Donor)	false
O1G	N	GLY- 336	2.71	152.94	H-Bond (Protein Donor)	false
O1A	N	LEU- 337	3.34	126.59	H-Bond (Protein Donor)	false
O2A	N	LEU- 337	3.29	151.68	H-Bond (Protein Donor)	false