scPDB - 1qin entry

Protein Data Bank Entry:

PDB ID : 1qin

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 1999-06-14

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Lactoylglutathione lyase
ID:	LGUL_HUMAN
AC:	Q04760
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	4.4.1.5

Chains:

Chain Name:	Percentage of Residues within binding site
A	49 %
B	51 %

Ligand binding site composition:

B-Factor:	23.654
Number of residues:	41
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
1.115	529.875

% Hydrophobic	% Polar
64.97	35.03
According to VolSite

Ligand :

HET Code:	GIP
Formula:	C17H21IN4O8S
Molecular weight:	568.340 g/mol
DrugBank ID:	DB03330
Buried Surface Area:	62.03 %
Polar Surface area:	237.93 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	4
Rings:	1
Aromatic rings:	1
Anionic atoms:	3
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
-4.80003	3.01527	35.0549

Binding mode :

What is Poseview ?

2D View
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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
OF2	NE2	GLN- 33	2.83	138.21	H-Bond (Protein Donor)	false
OT1	CZ	ARG- 37	3.73	0	Ionic (Protein Cationic)	false
OT2	CZ	ARG- 37	3.53	0	Ionic (Protein Cationic)	false
OT1	NE	ARG- 37	2.8	168.84	H-Bond (Protein Donor)	false
OT2	NH2	ARG- 37	2.92	139.36	H-Bond (Protein Donor)	false
OT2	NE	ARG- 37	3.31	131.31	H-Bond (Protein Donor)	false
CM2	SG	CYS- 60	4.21	0	Hydrophobic	false
I	SG	CYS- 60	4.39	0	Hydrophobic	false
I	CZ	PHE- 62	4.39	0	Hydrophobic	false
CB	CG	PHE- 67	3.61	0	Hydrophobic	false
CG	CE1	PHE- 67	3.82	0	Hydrophobic	false
SG2	CD1	LEU- 69	4.08	0	Hydrophobic	false
CL2	CD1	LEU- 69	3.3	0	Hydrophobic	false
I	CD1	LEU- 92	4.28	0	Hydrophobic	false
CZ	CD1	LEU- 92	3.97	0	Hydrophobic	false
CG	CG2	THR- 101	3.64	0	Hydrophobic	false
OT1	ND2	ASN- 103	2.96	165.65	H-Bond (Protein Donor)	false
N	OD1	ASN- 103	2.88	155.82	H-Bond (Ligand Donor)	false
OT1	CZ	ARG- 122	3.53	0	Ionic (Protein Cationic)	false
O31	N	LYS- 156	3.37	128.52	H-Bond (Protein Donor)	false
O32	N	LYS- 156	2.86	166.85	H-Bond (Protein Donor)	false
O31	N	MET- 157	2.83	155.83	H-Bond (Protein Donor)	false
SG2	SD	MET- 157	3.83	0	Hydrophobic	false
CL1	CD2	LEU- 160	3.68	0	Hydrophobic	false
CB2	CZ	PHE- 162	4.03	0	Hydrophobic	false
OF2	OE2	GLU- 172	3.47	123.98	H-Bond (Ligand Donor)	false
OF2	OE1	GLU- 172	2.54	160.84	H-Bond (Ligand Donor)	false
I	CB	MET- 179	4.19	0	Hydrophobic	false
CM1	CE	MET- 179	3.37	0	Hydrophobic	false
CM1	CD1	LEU- 182	3.99	0	Hydrophobic	false
I	CB	LEU- 182	4.44	0	Hydrophobic	false
I	CE	MET- 183	3.47	0	Hydrophobic	false
OF2	ZN	ZN- 301	2.09	0	Metal Acceptor	false
OZ1	ZN	ZN- 301	2.14	0	Metal Acceptor	false
N2	O	HOH- 404	2.97	163.65	H-Bond (Ligand Donor)	false