scPDB - 1q6p entry

Protein Data Bank Entry:

PDB ID : 1q6p

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2003-08-13

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Tyrosine-protein phosphatase non-receptor type 1
ID:	PTN1_HUMAN
AC:	P18031
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	3.1.3.48

Chains:

Chain Name:	Percentage of Residues within binding site
A	69 %
B	31 %

Ligand binding site composition:

B-Factor:	27.271
Number of residues:	42
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	2
Water Molecules:	1
Cofactors:
Metals:	CL

Cavity properties

Ligandability	Volume (Å3)
1.027	1478.250

% Hydrophobic	% Polar
44.06	55.94
According to VolSite

Ligand :

HET Code:	213
Formula:	C34H25F2N3O6P2
Molecular weight:	671.523 g/mol
DrugBank ID:	-
Buried Surface Area:	61.8 %
Polar Surface area:	176.71 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	0
Rings:	6
Aromatic rings:	6
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	10

Mass center Coordinates

X	Y	Z
37.4157	45.291	51.952

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
C35	CG	TYR- 546	3.47	0	Hydrophobic	false
C3	CE1	TYR- 546	3.39	0	Hydrophobic	false
N46	N	ASP- 548	3.18	160.69	H-Bond (Protein Donor)	false
C25	CB	ASP- 548	3.7	0	Hydrophobic	false
C35	CG2	VAL- 549	3.88	0	Hydrophobic	false
C10	CG2	VAL- 549	4.14	0	Hydrophobic	false
C25	CG2	VAL- 549	3.92	0	Hydrophobic	false
F53	CB	ASP- 681	4.01	0	Hydrophobic	false
F53	CE2	PHE- 682	3.54	0	Hydrophobic	false
F54	CE1	PHE- 682	3.49	0	Hydrophobic	false
C14	CZ	PHE- 682	3.41	0	Hydrophobic	false
O56	N	SER- 716	2.88	130.89	H-Bond (Protein Donor)	false
O56	N	ALA- 717	2.87	163.94	H-Bond (Protein Donor)	false
C10	CB	ALA- 717	3.45	0	Hydrophobic	false
C10	CD1	ILE- 719	4.07	0	Hydrophobic	false
C15	CG1	ILE- 719	3.9	0	Hydrophobic	false
C23	CD1	ILE- 719	4.13	0	Hydrophobic	false
C66	CD1	ILE- 719	4.21	0	Hydrophobic	false
O58	N	ILE- 719	3.06	154.95	H-Bond (Protein Donor)	false
O58	N	GLY- 720	2.65	169.21	H-Bond (Protein Donor)	false
O56	CZ	ARG- 721	3.83	0	Ionic (Protein Cationic)	false
O57	CZ	ARG- 721	3.55	0	Ionic (Protein Cationic)	false
O56	NH2	ARG- 721	2.91	161.06	H-Bond (Protein Donor)	false
O57	N	ARG- 721	3.07	172.38	H-Bond (Protein Donor)	false
O57	NE	ARG- 721	2.83	163.37	H-Bond (Protein Donor)	false
O57	NH2	ARG- 721	3.41	131.69	H-Bond (Protein Donor)	false
C64	CE	MET- 758	3.49	0	Hydrophobic	false
C15	CG	GLN- 762	4.34	0	Hydrophobic	false
F54	CG	GLN- 762	3.66	0	Hydrophobic	false
C6	CB	ALA- 1017	4.32	0	Hydrophobic	false
C44	CB	ALA- 1018	4.26	0	Hydrophobic	false
C6	CB	ALA- 1018	3.59	0	Hydrophobic	false
C32	CG	GLN- 1021	4.12	0	Hydrophobic	false
C44	CG	GLN- 1021	3.42	0	Hydrophobic	false
C20	CG	GLN- 1021	3.51	0	Hydrophobic	false
C45	CG	GLN- 1021	3.7	0	Hydrophobic	false
C45	CB	ASP- 1022	4.11	0	Hydrophobic	false
O74	NH2	ARG- 1024	3.28	144.55	H-Bond (Protein Donor)	false
O57	O	HOH- 3035	2.71	179.79	H-Bond (Protein Donor)	false