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Chlorine in PDB 4mh7: Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896

Enzymatic activity of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896

All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896, PDB code: 4mh7 was solved by W.Zhang, A.Mciver, M.A.Stashko, D.Deryckere, B.R.Branchford, D.Hunter, D.B.Kireev, M.J.Miley, J.Norris-Drouin, W.M.Stewart, M.Lee, S.Sather, Y.Zhou, J.A.Dipaola, M.Machius, W.P.Janzen, H.S.Earp, D.K.Graham, S.Frye, X.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.06 / 2.51
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.874, 90.864, 69.587, 90.00, 99.98, 90.00
R / Rfree (%) 22.3 / 27.9

Other elements in 4mh7:

The structure of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 (pdb code 4mh7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 8 binding sites of Chlorine where determined in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896, PDB code: 4mh7:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Chlorine binding site 1 out of 8 in 4mh7

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Chlorine binding site 1 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl901

b:24.7
occ:1.00
 H A:LYS820 2.3 29.7 1.0
HD2 A:PRO802 2.7 29.4 1.0
HD2 A:LYS820 2.9 39.5 1.0
HA A:LEU819 2.9 28.0 1.0
N A:LYS820 3.1 24.7 1.0
HD23 A:LEU819 3.1 27.0 1.0
HB2 A:LYS820 3.2 33.5 1.0
HA A:TYR801 3.2 30.4 1.0
HD13 B:LEU688 3.5 33.1 1.0
HZ2 A:TRP791 3.6 27.5 1.0
H A:TYR801 3.6 30.4 1.0
CD A:PRO802 3.7 24.5 1.0
HD22 A:LEU819 3.7 27.0 1.0
HG3 A:LYS820 3.7 36.2 1.0
HD11 B:LEU688 3.8 33.1 1.0
CA A:LEU819 3.8 23.4 1.0
CD A:LYS820 3.8 32.9 1.0
CB A:LYS820 3.8 28.0 1.0
CD2 A:LEU819 3.9 22.5 1.0
C A:LEU819 3.9 24.2 1.0
CG A:LYS820 4.0 30.1 1.0
CZ2 A:TRP791 4.0 22.9 1.0
HD3 A:PRO802 4.0 29.4 1.0
CA A:LYS820 4.0 25.5 1.0
CA A:TYR801 4.0 25.4 1.0
HG2 A:PRO802 4.0 28.7 1.0
CD1 B:LEU688 4.1 27.6 1.0
HB3 A:LEU819 4.1 29.1 1.0
N A:TYR801 4.2 25.3 1.0
CG A:PRO802 4.3 23.9 1.0
CB A:LEU819 4.4 24.3 1.0
HD1 A:TYR801 4.4 31.1 1.0
HD3 A:LYS820 4.4 39.5 1.0
HZ2 A:LYS820 4.4 43.0 1.0
HD22 B:LEU688 4.5 31.2 1.0
HE3 A:LYS820 4.5 40.9 1.0
HD21 A:LEU819 4.5 27.0 1.0
HG3 A:PRO802 4.6 28.7 1.0
N A:PRO802 4.6 25.2 1.0
HE1 A:TRP791 4.6 28.3 1.0
HD21 B:LEU688 4.6 31.2 1.0
O A:ARG818 4.6 24.3 1.0
CE2 A:TRP791 4.6 23.2 1.0
CH2 A:TRP791 4.6 24.0 1.0
HH2 A:TRP791 4.6 28.8 1.0
O A:LYS820 4.7 24.2 1.0
CE A:LYS820 4.7 34.1 1.0
HB3 A:LYS820 4.7 33.5 1.0
HH A:TYR812 4.7 34.0 1.0
HD12 B:LEU688 4.7 33.1 1.0
CG A:LEU819 4.7 23.4 1.0
CD1 A:TYR801 4.8 25.9 1.0
HA A:LYS820 4.8 30.6 1.0
C A:TYR801 4.8 25.7 1.0
C A:LYS820 4.8 25.6 1.0
NE1 A:TRP791 4.9 23.6 1.0
N A:LEU819 4.9 24.7 1.0
CD2 B:LEU688 4.9 26.0 1.0
HG2 A:LYS820 4.9 36.2 1.0

Chlorine binding site 2 out of 8 in 4mh7

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Chlorine binding site 2 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl902

b:24.7
occ:1.00
 O B:HOH1014 3.0 25.2 1.0
HA A:MET798 3.0 24.6 1.0
HA B:MET798 3.0 23.1 1.0
HG2 B:MET798 3.0 29.4 1.0
HG2 A:MET798 3.1 29.2 1.0
O B:HOH1005 3.1 18.8 1.0
O A:HOH1004 3.1 17.9 1.0
HH22 A:ARG687 3.3 34.9 1.0
HH11 B:ARG687 3.7 39.6 1.0
HH12 A:ARG687 3.7 36.3 1.0
CG B:MET798 3.8 24.5 1.0
HG3 B:MET798 3.8 29.4 1.0
CA A:MET798 3.9 20.5 1.0
CG A:MET798 3.9 24.4 1.0
HG3 A:MET798 3.9 29.2 1.0
CA B:MET798 3.9 19.2 1.0
HH12 B:ARG687 3.9 39.6 1.0
O A:GLY797 4.0 21.1 1.0
O B:GLY797 4.1 21.4 1.0
NH2 A:ARG687 4.1 29.1 1.0
NH1 B:ARG687 4.2 33.0 1.0
N A:MET798 4.2 20.9 1.0
N B:MET798 4.3 20.4 1.0
HD22 A:LEU684 4.3 27.1 1.0
C A:GLY797 4.3 20.5 1.0
HD21 A:LEU684 4.3 27.1 1.0
HD22 B:LEU684 4.3 26.2 1.0
HD21 B:LEU684 4.3 26.2 1.0
C B:GLY797 4.4 22.1 1.0
CB B:MET798 4.4 21.5 1.0
CB A:MET798 4.4 23.2 1.0
H B:THR799 4.4 23.3 1.0
H A:THR799 4.5 25.3 1.0
NH1 A:ARG687 4.5 30.2 1.0
CD2 B:LEU684 4.6 21.9 1.0
CD2 A:LEU684 4.7 22.6 1.0
HD23 B:LEU684 4.7 26.2 1.0
HH21 A:ARG687 4.7 34.9 1.0
HB3 B:MET798 4.7 25.8 1.0
H A:MET798 4.7 25.1 1.0
HD23 A:LEU684 4.7 27.1 1.0
H B:MET798 4.8 24.5 1.0
HB3 A:MET798 4.8 27.8 1.0
CZ A:ARG687 4.8 33.7 1.0
C A:MET798 5.0 19.5 1.0
O A:HOH1005 5.0 23.2 1.0
C B:MET798 5.0 21.4 1.0

Chlorine binding site 3 out of 8 in 4mh7

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Chlorine binding site 3 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl903

b:52.4
occ:1.00
 HD2 A:TYR685 3.2 39.9 1.0
HD1 A:TYR682 3.4 32.4 1.0
H172 A:MH7906 3.6 45.0 1.0
H171 A:MH7906 3.9 45.0 1.0
H173 A:MH7906 3.9 45.0 1.0
HA A:TYR676 4.0 37.7 1.0
HE1 A:TYR682 4.0 35.4 1.0
HD3 A:PRO692 4.0 47.9 1.0
C17 A:MH7906 4.0 37.5 1.0
HE2 A:TYR685 4.0 39.4 1.0
CD2 A:TYR685 4.1 33.3 1.0
O A:TYR676 4.1 31.7 1.0
CD1 A:TYR682 4.2 27.0 1.0
HD1 A:TYR676 4.2 46.7 1.0
CE1 A:TYR682 4.4 29.5 1.0
CE2 A:TYR685 4.5 32.9 1.0
HG3 A:PRO692 4.5 43.2 1.0
CA A:TYR676 4.8 31.4 1.0
C A:TYR676 4.8 30.4 1.0
HA A:TYR682 4.8 28.0 1.0
CD A:PRO692 4.8 39.9 1.0
HB3 A:TYR676 4.8 38.1 1.0
CD1 A:TYR676 5.0 38.9 1.0
HD2 A:PRO692 5.0 47.9 1.0

Chlorine binding site 4 out of 8 in 4mh7

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Chlorine binding site 4 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl904

b:30.0
occ:1.00
 H A:LEU589 2.3 35.5 1.0
HH22 A:ARG584 2.6 42.9 1.0
HA A:ILE588 3.0 37.2 1.0
N A:LEU589 3.2 29.6 1.0
HH12 A:ARG584 3.2 43.8 1.0
HB2 A:LEU589 3.2 37.6 1.0
NH2 A:ARG584 3.5 35.8 1.0
HG A:LEU589 3.6 40.3 1.0
HG23 A:ILE588 3.8 36.8 1.0
CA A:ILE588 3.8 31.0 1.0
CB A:LEU589 3.9 31.4 1.0
NH1 A:ARG584 3.9 36.5 1.0
HD13 A:ILE588 4.0 39.9 1.0
HD12 A:LEU589 4.0 45.8 1.0
C A:ILE588 4.0 30.5 1.0
HH21 A:ARG584 4.0 42.9 1.0
O A:LEU587 4.0 31.8 1.0
CA A:LEU589 4.0 30.5 1.0
CG A:LEU589 4.1 33.6 1.0
CZ A:ARG584 4.2 38.7 1.0
O A:LEU589 4.2 30.1 1.0
HD12 A:ILE588 4.3 39.9 1.0
CG2 A:ILE588 4.5 30.6 1.0
HG22 A:ILE588 4.5 36.8 1.0
CD1 A:LEU589 4.6 38.1 1.0
CD1 A:ILE588 4.6 33.3 1.0
C A:LEU589 4.6 29.7 1.0
HH11 A:ARG584 4.7 43.8 1.0
CB A:ILE588 4.7 30.6 1.0
HB3 A:LEU589 4.8 37.6 1.0
N A:ILE588 4.8 30.6 1.0
C A:LEU587 4.8 31.5 1.0
HA A:LEU589 4.9 36.6 1.0

Chlorine binding site 5 out of 8 in 4mh7

Go back to Chlorine Binding Sites List in 4mh7
Chlorine binding site 5 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl901

b:34.9
occ:1.00
 HH11 B:ARG651 2.0 49.0 1.0
HH12 B:ARG732 2.1 31.4 1.0
H B:ARG651 2.5 33.2 1.0
HH22 B:ARG732 2.5 30.4 1.0
HG2 B:ARG651 2.6 40.7 1.0
NH1 B:ARG651 2.7 40.9 1.0
HH12 B:ARG651 2.9 49.0 1.0
NH1 B:ARG732 2.9 26.1 1.0
HG3 B:PRO672 3.1 34.7 1.0
HA B:ILE650 3.2 32.6 1.0
HD3 B:ARG651 3.2 46.3 1.0
NH2 B:ARG732 3.2 25.4 1.0
N B:ARG651 3.3 27.6 1.0
HB3 B:ARG651 3.3 38.9 1.0
CG B:ARG651 3.3 33.9 1.0
CZ B:ARG732 3.5 26.8 1.0
HH11 B:ARG732 3.6 31.4 1.0
CD B:ARG651 3.7 38.6 1.0
CB B:ARG651 3.7 32.4 1.0
HG13 B:ILE650 3.7 34.6 1.0
HE1 B:MET674 3.7 38.9 1.0
CZ B:ARG651 3.8 41.1 1.0
CG B:PRO672 3.9 28.9 1.0
HH21 B:ARG732 4.0 30.4 1.0
CA B:ILE650 4.0 27.2 1.0
HG2 B:PRO672 4.0 34.7 1.0
O B:VAL649 4.1 25.8 1.0
CA B:ARG651 4.1 28.5 1.0
C B:ILE650 4.1 26.2 1.0
HG3 B:ARG651 4.1 40.7 1.0
NE B:ARG651 4.2 39.5 1.0
HE2 B:MET674 4.3 38.9 1.0
CE B:MET674 4.4 32.4 1.0
CG1 B:ILE650 4.5 28.9 1.0
HD2 B:ARG651 4.6 46.3 1.0
HG12 B:ILE650 4.6 34.6 1.0
HB2 B:ARG651 4.6 38.9 1.0
HE3 B:MET674 4.7 38.9 1.0
HB3 B:PRO672 4.7 31.0 1.0
CB B:PRO672 4.8 25.9 1.0
HA B:ARG651 4.8 34.2 1.0
HB2 B:PRO672 4.8 31.0 1.0
NE B:ARG732 4.8 26.9 1.0
CB B:ILE650 4.9 26.6 1.0
NH2 B:ARG651 4.9 38.1 1.0
C B:VAL649 4.9 23.9 1.0
HD3 B:PRO672 4.9 32.7 1.0
O B:ARG651 4.9 29.7 1.0
N B:ILE650 4.9 23.8 1.0
CD B:PRO672 5.0 27.3 1.0
HE B:ARG651 5.0 47.4 1.0

Chlorine binding site 6 out of 8 in 4mh7

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Chlorine binding site 6 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl902

b:24.1
occ:1.00
 H B:LYS820 2.4 29.1 1.0
HD2 B:PRO802 2.7 28.5 1.0
HD2 B:LYS820 2.9 40.6 1.0
HA B:LEU819 3.1 28.5 1.0
HD23 B:LEU819 3.1 24.2 1.0
HD13 A:LEU688 3.1 37.5 1.0
HB2 B:LYS820 3.2 32.0 1.0
HA B:TYR801 3.2 28.4 1.0
N B:LYS820 3.3 24.3 1.0
O B:HOH1009 3.4 24.8 1.0
HD11 A:LEU688 3.4 37.5 1.0
HZ2 B:TRP791 3.6 26.6 1.0
CD B:PRO802 3.6 23.8 1.0
H B:TYR801 3.7 28.3 1.0
HD22 B:LEU819 3.7 24.2 1.0
CD1 A:LEU688 3.7 31.2 1.0
HG3 B:LYS820 3.7 36.5 1.0
CD B:LYS820 3.8 33.8 1.0
CD2 B:LEU819 3.8 20.1 1.0
CB B:LYS820 3.9 26.6 1.0
CA B:LEU819 3.9 23.7 1.0
HG2 B:PRO802 3.9 31.4 1.0
CG B:LYS820 4.0 30.4 1.0
CZ2 B:TRP791 4.0 22.2 1.0
HD3 B:PRO802 4.0 28.5 1.0
HD12 A:LEU688 4.1 37.5 1.0
CA B:TYR801 4.1 23.7 1.0
C B:LEU819 4.1 23.8 1.0
CA B:LYS820 4.2 27.0 1.0
HB3 B:LEU819 4.2 28.9 1.0
CG B:PRO802 4.3 26.1 1.0
N B:TYR801 4.3 23.6 1.0
HZ2 B:LYS820 4.3 43.6 1.0
HD3 B:LYS820 4.4 40.6 1.0
HE3 B:LYS820 4.4 41.2 1.0
HD21 B:LEU819 4.5 24.2 1.0
CB B:LEU819 4.5 24.1 1.0
HG3 B:PRO802 4.5 31.4 1.0
HD1 B:TYR801 4.5 28.6 1.0
HH2 B:TRP791 4.5 27.0 1.0
N B:PRO802 4.5 23.6 1.0
CH2 B:TRP791 4.6 22.5 1.0
CE B:LYS820 4.6 34.3 1.0
CE2 B:TRP791 4.7 21.5 1.0
HD22 A:LEU688 4.7 36.2 1.0
O B:ARG818 4.7 22.9 1.0
O B:LYS820 4.8 27.7 1.0
HB3 B:LYS820 4.8 32.0 1.0
CG B:LEU819 4.8 23.0 1.0
HE1 B:TRP791 4.8 28.7 1.0
C B:TYR801 4.8 26.0 1.0
HH B:TYR812 4.9 31.4 1.0
NZ B:LYS820 4.9 36.3 1.0
HD21 A:LEU688 4.9 36.2 1.0
CD1 B:TYR801 4.9 23.9 1.0
HA B:LYS820 4.9 32.4 1.0
C B:LYS820 5.0 28.0 1.0
HG2 B:LYS820 5.0 36.5 1.0
CG A:LEU688 5.0 31.5 1.0

Chlorine binding site 7 out of 8 in 4mh7

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Chlorine binding site 7 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl903

b:43.3
occ:1.00
 H B:LEU589 2.5 40.7 1.0
HH22 B:ARG584 2.6 49.2 1.0
HB2 B:LEU589 3.2 44.7 1.0
HA B:ILE588 3.2 41.5 1.0
HH12 B:ARG584 3.3 47.7 1.0
N B:LEU589 3.3 33.9 1.0
NH2 B:ARG584 3.5 41.0 1.0
HG B:LEU589 3.5 46.2 1.0
HD12 B:LEU589 3.8 52.0 1.0
CB B:LEU589 3.9 37.3 1.0
NH1 B:ARG584 4.0 39.7 1.0
HH21 B:ARG584 4.0 49.2 1.0
CA B:ILE588 4.1 34.6 1.0
CG B:LEU589 4.1 38.5 1.0
O B:LEU587 4.1 36.4 1.0
CA B:LEU589 4.1 34.5 1.0
HG23 B:ILE588 4.1 39.5 1.0
C B:ILE588 4.2 32.8 1.0
CZ B:ARG584 4.2 43.6 1.0
HD13 B:ILE588 4.3 48.5 1.0
O B:LEU589 4.3 33.5 1.0
CD1 B:LEU589 4.4 43.4 1.0
HD12 B:ILE588 4.7 48.5 1.0
HB3 B:LEU589 4.7 44.7 1.0
C B:LEU589 4.7 31.6 1.0
HH11 B:ARG584 4.8 47.7 1.0
CG2 B:ILE588 4.8 32.9 1.0
HG22 B:ILE588 4.8 39.5 1.0
C B:LEU587 4.9 35.8 1.0
HD11 B:LEU589 4.9 52.0 1.0
HA B:LEU589 4.9 41.5 1.0
N B:ILE588 4.9 32.8 1.0
CD1 B:ILE588 5.0 40.4 1.0

Chlorine binding site 8 out of 8 in 4mh7

Go back to Chlorine Binding Sites List in 4mh7
Chlorine binding site 8 out of 8 in the Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Crystal Structure of the Catalytic Domain of the Proto-Oncogene Tyrosine-Protein Kinase Mer in Complex with Inhibitor UNC1896 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl904

b:47.5
occ:1.00
 HD2 B:TYR682 3.5 31.6 1.0
HA B:TYR676 3.6 29.9 1.0
HD1 B:TYR676 3.8 37.7 1.0
O B:TYR676 3.8 27.0 1.0
HE2 B:TYR682 4.1 33.2 1.0
HD2 B:TYR685 4.1 37.1 1.0
HB3 B:TYR676 4.2 28.8 1.0
CD2 B:TYR682 4.3 26.3 1.0
CA B:TYR676 4.4 25.0 1.0
CD1 B:TYR676 4.4 31.4 1.0
HG3 B:PRO692 4.4 35.6 1.0
C B:TYR676 4.5 24.2 1.0
CE2 B:TYR682 4.6 27.7 1.0
CB B:TYR676 4.7 24.0 1.0
HG2 B:PRO692 4.8 35.6 1.0
HD3 B:PRO692 4.8 37.5 1.0
HE2 B:TYR685 4.8 34.6 1.0
CG B:TYR676 4.9 27.4 1.0
CD2 B:TYR685 4.9 30.9 1.0

Reference:

W.Zhang, A.L.Mciver, M.A.Stashko, D.Deryckere, B.R.Branchford, D.Hunter, D.Kireev, M.J.Miley, J.Norris-Drouin, W.M.Stewart, M.Lee, S.Sather, Y.Zhou, J.A.Di Paola, M.Machius, W.P.Janzen, H.S.Earp, D.K.Graham, S.V.Frye, X.Wang. Discovery of Mer Specific Tyrosine Kinase Inhibitors For the Treatment and Prevention of Thrombosis. J.Med.Chem. V. 56 9693 2013.
ISSN: ISSN 0022-2623
PubMed: 24219778
DOI: 10.1021/JM4013888
Page generated: Sun Jul 21 19:51:37 2024

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