scPDB - 1s9j entry

Protein Data Bank Entry:

PDB ID : 1s9j

Resolution :2.400 Å

Experimental Method : X-ray

Deposition Date : 2004-02-04

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:	20.892
Number of residues:	36
Including
Standard Amino Acids:	34
Non Standard Amino Acids:	2
Water Molecules:	0
Cofactors:	ATP
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
1.163	1242.000

% Hydrophobic	% Polar
43.75	56.25
According to VolSite

Ligand :

HET Code:	BBM
Formula:	C16H13BrF3IN2O4
Molecular weight:	561.089 g/mol
DrugBank ID:	DB03115
Buried Surface Area:	69.8 %
Polar Surface area:	90.82 Å2

Number of
H-Bond Acceptors:	5
H-Bond Donors:	4
Rings:	2
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
31.5629	27.8888	40.4863

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
O3	O	GLY- 77	3.01	127.99	H-Bond (Ligand Donor)	false
O4	NZ	LYS- 97	2.87	123.38	H-Bond (Protein Donor)	false
O2	NZ	LYS- 97	2.88	139.69	H-Bond (Protein Donor)	false
F3	CD	LYS- 97	3.67	0	Hydrophobic	false
C12	CD2	LEU- 115	4.27	0	Hydrophobic	false
F2	CG	LEU- 115	4.45	0	Hydrophobic	false
F2	CD1	LEU- 118	4.32	0	Hydrophobic	false
C4	CD1	LEU- 118	4.39	0	Hydrophobic	false
C5	CD2	LEU- 118	3.85	0	Hydrophobic	false
I	CB	VAL- 127	4	0	Hydrophobic	false
C3	CD1	ILE- 141	3.96	0	Hydrophobic	false
F2	CD1	ILE- 141	4.06	0	Hydrophobic	false
F3	CG2	ILE- 141	3.25	0	Hydrophobic	false
C1	SD	MET- 143	3.76	0	Hydrophobic	false
F3	CE	MET- 143	3.51	0	Hydrophobic	false
C6	CB	CYS- 207	4.47	0	Hydrophobic	false
I	CB	CYS- 207	4.48	0	Hydrophobic	false
C8	CB	ASP- 208	4.34	0	Hydrophobic	false
I	CE2	PHE- 209	4.13	0	Hydrophobic	false
F1	CG2	VAL- 211	4.03	0	Hydrophobic	false
F2	CG2	VAL- 211	3.59	0	Hydrophobic	false
F1	CB	SER- 212	4.15	0	Hydrophobic	false
C11	CD1	LEU- 215	3.81	0	Hydrophobic	false
C12	CD1	LEU- 215	3.91	0	Hydrophobic	false
BR	CG1	ILE- 216	3.44	0	Hydrophobic	false
C9	CE	MET- 219	3.58	0	Hydrophobic	false