scPDB - 2qme entry

Protein Data Bank Entry:

PDB ID : 2qme

Resolution :1.750 Å

Experimental Method : X-ray

Deposition Date : 2007-07-16

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Ras-related C3 botulinum toxin substrate 3
ID:	RAC3_HUMAN
AC:	P60763
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	25.851
Number of residues:	37
Including
Standard Amino Acids:	34
Non Standard Amino Acids:	1
Water Molecules:	2
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
0.284	351.000

% Hydrophobic	% Polar
54.81	45.19
According to VolSite

Ligand :

HET Code:	GCP
Formula:	C11H14N5O13P3
Molecular weight:	517.176 g/mol
DrugBank ID:	DB03725
Buried Surface Area:	70.73 %
Polar Surface area:	326.33 Å2

Number of
H-Bond Acceptors:	16
H-Bond Donors:	4
Rings:	3
Aromatic rings:	1
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
-10.5287	7.72069	22.5957

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
O1B	N	GLY- 15	3.08	157.88	H-Bond (Protein Donor)	false
O2G	NZ	LYS- 16	2.71	157.07	H-Bond (Protein Donor)	false
O1B	N	LYS- 16	3.08	157.46	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 16	2.73	153.23	H-Bond (Protein Donor)	false
O2G	NZ	LYS- 16	2.71	0	Ionic (Protein Cationic)	false
O1B	NZ	LYS- 16	2.73	0	Ionic (Protein Cationic)	false
O2B	N	THR- 17	2.97	161.13	H-Bond (Protein Donor)	false
O1A	N	CYS- 18	2.82	163.42	H-Bond (Protein Donor)	false
C2'	SG	CYS- 18	3.82	0	Hydrophobic	false
C2'	CZ	PHE- 28	4.08	0	Hydrophobic	false
C3B	CE1	TYR- 32	3.87	0	Hydrophobic	false
C5'	CD1	TYR- 32	3.88	0	Hydrophobic	false
C4'	CG	TYR- 32	4.25	0	Hydrophobic	false
C3'	CB	TYR- 32	3.96	0	Hydrophobic	false
O1G	N	THR- 35	2.77	154.09	H-Bond (Protein Donor)	false
O2G	N	GLY- 60	2.78	142.52	H-Bond (Protein Donor)	false
O4'	NZ	LYS- 116	3.04	122.73	H-Bond (Protein Donor)	false
N1	OD1	ASP- 118	2.8	164.97	H-Bond (Ligand Donor)	false
N2	OD2	ASP- 118	2.85	169.91	H-Bond (Ligand Donor)	false
O6	N	LEU- 160	3.24	146.48	H-Bond (Protein Donor)	false
O1G	MG	MG- 179	1.97	0	Metal Acceptor	false
O2B	MG	MG- 179	2.04	0	Metal Acceptor	false
O2A	O	HOH- 319	2.81	179.98	H-Bond (Protein Donor)	false
O3G	O	HOH- 347	2.94	162.2	H-Bond (Protein Donor)	false