scPDB - 3fzt entry

Protein Data Bank Entry:

PDB ID : 3fzt

Resolution :1.950 Å

Experimental Method : X-ray

Deposition Date : 2009-01-26

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Protein-tyrosine kinase 2-beta
ID:	FAK2_HUMAN
AC:	Q14289
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.7.10.2

Chains:

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

Ligand binding site composition:

B-Factor:	18.927
Number of residues:	36
Including
Standard Amino Acids:	35
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.392	1107.000

% Hydrophobic	% Polar
59.45	40.55
According to VolSite

Ligand :

HET Code:	4JZ
Formula:	C24H27N7O2
Molecular weight:	445.517 g/mol
DrugBank ID:	-
Buried Surface Area:	70.69 %
Polar Surface area:	107.53 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	3
Rings:	4
Aromatic rings:	3
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	6

Mass center Coordinates

X	Y	Z
-4.75188	-2.58003	11.6857

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
C6	CD1	LEU- 431	4.12	0	Hydrophobic	false
N25	NZ	LYS- 457	2.92	164.08	H-Bond (Protein Donor)	false
N29	OE2	GLU- 474	2.71	133.97	H-Bond (Ligand Donor)	false
N30	OE2	GLU- 474	2.85	135.35	H-Bond (Ligand Donor)	false
C16	CB	GLU- 474	3.86	0	Hydrophobic	false
C7	CG	GLU- 474	3.73	0	Hydrophobic	false
C8	CD1	ILE- 477	3.81	0	Hydrophobic	false
C1	CD1	ILE- 477	4.19	0	Hydrophobic	false
C10	CG2	ILE- 477	4.31	0	Hydrophobic	false
C2	SD	MET- 478	4.42	0	Hydrophobic	false
C10	SD	MET- 478	3.93	0	Hydrophobic	false
C2	CD1	LEU- 481	3.79	0	Hydrophobic	false
C2	CG2	ILE- 486	3.76	0	Hydrophobic	false
C3	CG2	ILE- 486	4.27	0	Hydrophobic	false
N26	N	TYR- 505	2.78	177.08	H-Bond (Protein Donor)	false
C4	CD1	LEU- 540	3.76	0	Hydrophobic	false
C2	CD2	LEU- 540	4.15	0	Hydrophobic	false
C5	CD2	LEU- 556	3.6	0	Hydrophobic	false
C15	CD1	LEU- 556	4.19	0	Hydrophobic	false
C18	CD1	LEU- 556	3.31	0	Hydrophobic	false
C3	CG	LEU- 565	3.93	0	Hydrophobic	false
O32	N	ASP- 567	2.86	168.46	H-Bond (Protein Donor)	false
C3	CB	ASP- 567	4.17	0	Hydrophobic	false
C15	CG	PHE- 568	3.63	0	Hydrophobic	false
DuAr	CZ	ARG- 572	3.73	27.97	Pi/Cation	false
C9	CD	ARG- 572	3.94	0	Hydrophobic	false
C8	CB	ASP- 576	3.87	0	Hydrophobic	false
N28	O	HOH- 1011	2.93	179.97	H-Bond (Protein Donor)	false