scPDB - 3os3 entry

Protein Data Bank Entry:

PDB ID : 3os3

Resolution :2.800 Å

Experimental Method : X-ray

Deposition Date : 2010-09-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Dual specificity mitogen-activated protein kinase kinase 1
ID:	MP2K1_HUMAN
AC:	Q02750
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.7.12.2

Chains:

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

Ligand binding site composition:

B-Factor:	55.914
Number of residues:	41
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	2
Water Molecules:	0
Cofactors:	ATP
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
1.205	1174.500

% Hydrophobic	% Polar
42.53	57.47
According to VolSite

Ligand :

HET Code:	3OS
Formula:	C20H18F3N3O5
Molecular weight:	437.369 g/mol
DrugBank ID:	-
Buried Surface Area:	72.28 %
Polar Surface area:	112.41 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	4
Rings:	2
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	10

Mass center Coordinates

X	Y	Z
9.56042	40.2154	-4.05632

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
O31	O1A	ATP- 1	3.41	147.82	H-Bond (Ligand Donor)	false
F18	CD	LYS- 97	3.59	0	Hydrophobic	false
C30	CD	LYS- 97	4.24	0	Hydrophobic	false
O26	NZ	LYS- 97	2.82	158.55	H-Bond (Protein Donor)	false
C30	CG1	ILE- 99	3.98	0	Hydrophobic	false
F10	CD2	LEU- 115	3.88	0	Hydrophobic	false
C11	CD1	LEU- 118	4.36	0	Hydrophobic	false
C12	CD2	LEU- 118	3.83	0	Hydrophobic	false
C13	CD1	LEU- 118	3.87	0	Hydrophobic	false
C14	CD2	LEU- 118	3.89	0	Hydrophobic	false
C15	CG2	ILE- 126	4.21	0	Hydrophobic	false
C15	CB	VAL- 127	4.19	0	Hydrophobic	false
C15	CB	PHE- 129	4.18	0	Hydrophobic	false
C3	CD1	ILE- 141	4.03	0	Hydrophobic	false
F18	CD1	ILE- 141	3.32	0	Hydrophobic	false
C17	CG2	ILE- 141	3.8	0	Hydrophobic	false
C16	SD	MET- 143	4.11	0	Hydrophobic	false
F18	CE	MET- 143	3.95	0	Hydrophobic	false
C23	CG	ARG- 189	3.61	0	Hydrophobic	false
C14	CE1	PHE- 209	3.67	0	Hydrophobic	false
F10	CG1	VAL- 211	3.41	0	Hydrophobic	false
F8	CB	SER- 212	4.21	0	Hydrophobic	false
C6	CG	LEU- 215	3.78	0	Hydrophobic	false
C1	CD2	LEU- 215	4.05	0	Hydrophobic	false
C7	CD2	LEU- 215	3.46	0	Hydrophobic	false
F8	CG1	ILE- 216	3.92	0	Hydrophobic	false
C19	CG1	ILE- 216	3.8	0	Hydrophobic	false
C5	CE	MET- 219	4.27	0	Hydrophobic	false
C22	CB	MET- 219	3.66	0	Hydrophobic	false
C19	CG	MET- 219	4.06	0	Hydrophobic	false
C29	CE	MET- 219	3.7	0	Hydrophobic	false