scPDB - 4hj2 entry

Protein Data Bank Entry:

PDB ID : 4hj2

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 2012-10-12

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
A	89 %
B	11 %

Ligand binding site composition:

B-Factor:	31.014
Number of residues:	39
Including
Standard Amino Acids:	35
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.037	1356.750

% Hydrophobic	% Polar
42.79	57.21
According to VolSite

Ligand :

HET Code:	LZ6
Formula:	C24H33ClN4O8S
Molecular weight:	573.059 g/mol
DrugBank ID:	-
Buried Surface Area:	56.22 %
Polar Surface area:	234.77 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	3
Rings:	1
Aromatic rings:	1
Anionic atoms:	3
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	20

Mass center Coordinates

X	Y	Z
20.2982	-9.07032	22.1642

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
S13	CE1	TYR- 9	4.14	0	Hydrophobic	false
C12	CZ	TYR- 9	3.54	0	Hydrophobic	false
C12	CE1	PHE- 10	4.26	0	Hydrophobic	false
S13	CD	ARG- 15	3.59	0	Hydrophobic	false
C32	CD	ARG- 15	3.96	0	Hydrophobic	false
C32	CB	GLN- 54	4.22	0	Hydrophobic	false
O26	NE2	GLN- 54	3.12	171.84	H-Bond (Protein Donor)	false
N29	O	VAL- 55	2.71	145.58	H-Bond (Ligand Donor)	false
O28	N	VAL- 55	3.27	159.96	H-Bond (Protein Donor)	false
O37	N	THR- 68	3.01	160.44	H-Bond (Protein Donor)	false
O37	OG1	THR- 68	3.3	132.71	H-Bond (Protein Donor)	false
O36	OG1	THR- 68	2.65	166.41	H-Bond (Protein Donor)	false
N38	OD2	ASP- 101	2.87	164.4	H-Bond (Ligand Donor)	false
N38	OD1	ASP- 101	3.13	134.1	H-Bond (Ligand Donor)	false
N38	OD2	ASP- 101	2.87	0	Ionic (Ligand Cationic)	false
N38	OD1	ASP- 101	3.13	0	Ionic (Ligand Cationic)	false
C4	CD1	LEU- 107	3.56	0	Hydrophobic	false
C14	CD1	LEU- 107	3.34	0	Hydrophobic	false
C3	CD2	LEU- 108	3.94	0	Hydrophobic	false
C16	CB	PRO- 110	3.24	0	Hydrophobic	false
C15	CG2	VAL- 111	4.38	0	Hydrophobic	false
C3	CG2	VAL- 111	3.89	0	Hydrophobic	false
O27	CZ	ARG- 131	3.5	0	Ionic (Protein Cationic)	false
O26	CZ	ARG- 131	3.74	0	Ionic (Protein Cationic)	false
O27	NH2	ARG- 131	2.74	171.15	H-Bond (Protein Donor)	false
O27	NH1	ARG- 131	3.39	130.64	H-Bond (Protein Donor)	false
O26	NH1	ARG- 131	2.89	154.43	H-Bond (Protein Donor)	false
C16	CB	MET- 208	3.46	0	Hydrophobic	false
C5	CE	MET- 208	3.38	0	Hydrophobic	false
C14	CE	MET- 208	3.57	0	Hydrophobic	false
C20	CE1	PHE- 220	3.68	0	Hydrophobic	false
CL10	CB	PHE- 220	3.55	0	Hydrophobic	false
C11	CE2	PHE- 220	3.36	0	Hydrophobic	false
O37	O	HOH- 447	2.84	179.95	H-Bond (Protein Donor)	false