scPDB - 2ofv entry

Protein Data Bank Entry:

PDB ID : 2ofv

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2007-01-04

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Tyrosine-protein kinase Lck
ID:	LCK_HUMAN
AC:	P06239
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.7.10.2

Chains:

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

Ligand binding site composition:

B-Factor:	21.386
Number of residues:	39
Including
Standard Amino Acids:	37
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.158	344.250

% Hydrophobic	% Polar
66.67	33.33
According to VolSite

Ligand :

HET Code:	242
Formula:	C23H17F3N4O
Molecular weight:	422.402 g/mol
DrugBank ID:	DB06925
Buried Surface Area:	82.76 %
Polar Surface area:	80.9 Å2

Number of
H-Bond Acceptors:	4
H-Bond Donors:	2
Rings:	4
Aromatic rings:	4
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	4

Mass center Coordinates

X	Y	Z
120.52	57.8305	15.257

Binding mode :

What is Poseview ?

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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
C11	CD1	LEU- 251	4.47	0	Hydrophobic	false
C11	CG1	VAL- 259	3.48	0	Hydrophobic	false
C25	CB	ALA- 271	3.82	0	Hydrophobic	false
C2	CB	ALA- 271	3.39	0	Hydrophobic	false
C19	CD	LYS- 273	4.34	0	Hydrophobic	false
C25	CB	LYS- 273	3.78	0	Hydrophobic	false
N31	OE2	GLU- 288	2.84	129.06	H-Bond (Ligand Donor)	false
C37	CG	GLU- 288	3.41	0	Hydrophobic	false
C35	CD2	LEU- 291	3.87	0	Hydrophobic	false
C33	CG	MET- 292	3.93	0	Hydrophobic	false
C37	CG	MET- 292	4.36	0	Hydrophobic	false
C19	CE	MET- 292	3.42	0	Hydrophobic	false
F1	CD1	LEU- 295	3.8	0	Hydrophobic	false
F2	CG	LEU- 300	4.03	0	Hydrophobic	false
F1	CD2	LEU- 300	3.65	0	Hydrophobic	false
C8	CG2	VAL- 301	4.15	0	Hydrophobic	false
C17	CG1	VAL- 301	4.22	0	Hydrophobic	false
C20	CG2	ILE- 314	3.49	0	Hydrophobic	false
C8	CB	THR- 316	4.31	0	Hydrophobic	false
C25	CG2	THR- 316	3.95	0	Hydrophobic	false
C21	CG2	THR- 316	3.63	0	Hydrophobic	false
C20	CG2	THR- 316	3.62	0	Hydrophobic	false
N3	N	MET- 319	2.9	174.13	H-Bond (Protein Donor)	false
N15	O	MET- 319	2.92	160.22	H-Bond (Ligand Donor)	false
F3	CD1	ILE- 355	3.86	0	Hydrophobic	false
F3	CE2	TYR- 360	3.82	0	Hydrophobic	false
C2	CD2	LEU- 371	3.69	0	Hydrophobic	false
F3	CG2	ILE- 380	4.36	0	Hydrophobic	false
F2	CG2	ILE- 380	3.52	0	Hydrophobic	false
C17	CB	ALA- 381	4.4	0	Hydrophobic	false
O30	N	ASP- 382	2.74	145.99	H-Bond (Protein Donor)	false
C37	CB	ASP- 382	3.9	0	Hydrophobic	false
C10	CB	PHE- 383	3.84	0	Hydrophobic	false
C17	CB	PHE- 383	4.4	0	Hydrophobic	false
C36	CG2	ILE- 389	3.55	0	Hydrophobic	false
C37	CG1	ILE- 389	4.04	0	Hydrophobic	false