scPDB - 3ik9 entry

Protein Data Bank Entry:

PDB ID : 3ik9

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2009-08-05

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Glutathione S-transferase A1
ID:	GSTA1_HUMAN
AC:	P08263
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.5.1.18

Chains:

Chain Name:	Percentage of Residues within binding site
G	13 %
H	87 %

Ligand binding site composition:

B-Factor:	41.559
Number of residues:	31
Including
Standard Amino Acids:	31
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.491	1869.750

% Hydrophobic	% Polar
45.31	54.69
According to VolSite

Ligand :

HET Code:	BOB
Formula:	C19H34N3O8S
Molecular weight:	464.554 g/mol
DrugBank ID:	-
Buried Surface Area:	57.18 %
Polar Surface area:	231.86 Å2

Number of
H-Bond Acceptors:	9
H-Bond Donors:	5
Rings:	0
Aromatic rings:	0
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	1
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
40.3607	-36.4407	-7.86181

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
SG2	CZ	TYR- 9	4.32	0	Hydrophobic	false
C54	CE1	PHE- 10	4.01	0	Hydrophobic	false
CB2	CE1	PHE- 10	4.01	0	Hydrophobic	false
O60	NE	ARG- 15	3.29	166.46	H-Bond (Protein Donor)	false
SG2	CD	ARG- 15	3.61	0	Hydrophobic	false
CG1	CD	ARG- 15	3.8	0	Hydrophobic	false
O32	NE2	GLN- 54	3.01	157.83	H-Bond (Protein Donor)	false
CG1	CB	GLN- 54	4.17	0	Hydrophobic	false
N2	O	VAL- 55	2.63	172.81	H-Bond (Ligand Donor)	false
O2	N	VAL- 55	2.99	148.04	H-Bond (Protein Donor)	false
CB2	CG2	VAL- 55	4.31	0	Hydrophobic	false
O11	N	THR- 68	3.26	141.19	H-Bond (Protein Donor)	false
O11	OG1	THR- 68	2.8	167.45	H-Bond (Protein Donor)	false
O12	N	THR- 68	3.31	162.64	H-Bond (Protein Donor)	false
O12	OG1	THR- 68	3.41	126.77	H-Bond (Protein Donor)	false
N1	OD1	ASP- 101	3.25	121.13	H-Bond (Ligand Donor)	false
N1	OD2	ASP- 101	2.75	170.88	H-Bond (Ligand Donor)	false
N1	OD1	ASP- 101	3.25	0	Ionic (Ligand Cationic)	false
N1	OD2	ASP- 101	2.75	0	Ionic (Ligand Cationic)	false
C42	SD	MET- 108	4.19	0	Hydrophobic	false
C44	CE2	PHE- 111	3.76	0	Hydrophobic	false
C45	CD2	PHE- 111	4.09	0	Hydrophobic	false
C46	CE2	PHE- 111	4.41	0	Hydrophobic	false
C54	CZ	PHE- 111	4.03	0	Hydrophobic	false
C55	CE1	PHE- 111	3.61	0	Hydrophobic	false
O31	CZ	ARG- 131	3.83	0	Ionic (Protein Cationic)	false
O31	NH2	ARG- 131	3.11	169.77	H-Bond (Protein Donor)	false
O32	NH1	ARG- 131	3.16	160.03	H-Bond (Protein Donor)	false
C55	CE1	TYR- 212	3.78	0	Hydrophobic	false
O56	OH	TYR- 212	2.6	157.23	H-Bond (Ligand Donor)	false
C44	CG1	VAL- 216	3.87	0	Hydrophobic	false
C54	CG1	VAL- 216	3.81	0	Hydrophobic	false
C55	CG2	VAL- 216	4.34	0	Hydrophobic	false
C47	CE1	TYR- 217	4.08	0	Hydrophobic	false
C46	CD2	PHE- 220	3.94	0	Hydrophobic	false
CB2	CZ	PHE- 220	4.06	0	Hydrophobic	false
C43	CE2	PHE- 220	4.3	0	Hydrophobic	false