Fluorine in PDB 6o5z: Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2

The structure of Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2, PDB code: 6o5z was solved by A.D.Cowan, J.M.Murphy, C.L.Pierotti, G.L.Lessene, P.E.Czabotar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.10 / 2.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.161, 118.845, 52.761, 90.00, 116.78, 90.00
R / Rfree (%)	18.3 / 23.2

The binding sites of Fluorine atom in the Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2 (pdb code 6o5z). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2, PDB code: 6o5z:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:94.5 occ:1.00 F01 B:LN4501 0.0 94.5 1.0 C04 B:LN4501 1.3 90.0 1.0 C05 B:LN4501 2.3 90.7 1.0 C03 B:LN4501 2.4 82.7 1.0 N08 B:LN4501 2.8 74.2 1.0 CG B:GLU250 3.1 51.4 1.0 CD B:GLU250 3.5 57.8 1.0 C06 B:LN4501 3.6 89.4 1.0 C02 B:LN4501 3.6 83.7 1.0 O B:GLY349 3.7 89.2 1.0 OE1 B:GLU250 3.9 63.3 1.0 C09 B:LN4501 4.0 68.1 1.0 CB B:GLU250 4.0 52.2 1.0 OE2 B:GLU250 4.0 59.4 1.0 C07 B:LN4501 4.1 87.1 1.0 CA B:GLU250 4.3 53.1 1.0 O11 B:LN4501 4.5 68.7 1.0 C B:GLY349 4.7 85.5 1.0 N10 B:LN4501 4.9 63.9 1.0 CA B:GLY349 5.0 72.7 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:88.5 occ:1.00 F38 B:LN4501 0.0 88.5 1.0 C37 B:LN4501 1.3 87.5 1.0 F39 B:LN4501 2.1 87.6 1.0 F40 B:LN4501 2.1 86.7 1.0 C07 B:LN4501 2.4 87.1 1.0 C06 B:LN4501 3.2 89.4 1.0 C02 B:LN4501 3.3 83.7 1.0 CG2 B:THR253 3.6 34.5 1.0 CG2 B:ILE262 4.1 25.8 1.0 O B:THR253 4.2 39.8 1.0 C B:THR253 4.5 42.2 1.0 C05 B:LN4501 4.5 90.7 1.0 CD1 B:LEU320 4.5 37.1 1.0 CD1 B:ILE262 4.6 25.9 1.0 C03 B:LN4501 4.6 82.7 1.0 CA B:MET254 4.6 44.9 1.0 N B:MET254 4.6 44.8 1.0 CB B:THR253 4.7 40.5 1.0 CG B:MET254 4.7 51.8 1.0 CD2 B:PHE257 4.8 39.7 1.0 CB B:PHE257 4.9 33.9 1.0 C04 B:LN4501 5.0 90.0 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:87.6 occ:1.00 F39 B:LN4501 0.0 87.6 1.0 C37 B:LN4501 1.3 87.5 1.0 F38 B:LN4501 2.1 88.5 1.0 F40 B:LN4501 2.1 86.7 1.0 C07 B:LN4501 2.4 87.1 1.0 C02 B:LN4501 2.9 83.7 1.0 O B:LEU347 3.4 30.8 1.0 CA B:ALA348 3.4 58.6 1.0 C06 B:LN4501 3.6 89.4 1.0 C B:ALA348 3.7 55.9 1.0 C B:LEU347 3.8 32.8 1.0 N B:ALA348 3.9 61.6 1.0 O B:ALA348 4.0 52.8 1.0 N B:GLY349 4.2 63.5 1.0 CG2 B:ILE262 4.3 25.8 1.0 C03 B:LN4501 4.3 82.7 1.0 CG B:LEU347 4.4 35.4 1.0 CD1 B:ILE262 4.5 25.9 1.0 CB B:ALA348 4.7 61.1 1.0 O11 B:LN4501 4.7 68.7 1.0 C05 B:LN4501 4.8 90.7 1.0 CD2 B:HIS329 4.8 33.0 1.0 CB B:LEU347 4.8 30.9 1.0 NE2 B:HIS329 4.8 32.5 1.0 CA B:LEU347 4.9 30.4 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of the Human Mlkl Pseudokinase Domain Bound to Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:86.7 occ:1.00 F40 B:LN4501 0.0 86.7 1.0 C37 B:LN4501 1.3 87.5 1.0 F39 B:LN4501 2.1 87.6 1.0 F38 B:LN4501 2.1 88.5 1.0 C07 B:LN4501 2.4 87.1 1.0 C06 B:LN4501 2.8 89.4 1.0 CD2 B:HIS329 3.5 33.0 1.0 C02 B:LN4501 3.6 83.7 1.0 CD2 B:LEU320 3.9 35.5 1.0 NE2 B:HIS329 4.0 32.5 1.0 C05 B:LN4501 4.1 90.7 1.0 CD1 B:LEU320 4.3 37.1 1.0 O B:ALA348 4.5 52.8 1.0 CG2 B:THR253 4.5 34.5 1.0 CG B:LEU320 4.5 37.1 1.0 C B:ALA348 4.6 55.9 1.0 CG B:HIS329 4.6 35.2 1.0 CG B:LEU347 4.6 35.4 1.0 CD2 B:LEU347 4.7 37.7 1.0 C03 B:LN4501 4.8 82.7 1.0 CA B:ALA348 4.9 58.6 1.0 C04 B:LN4501 5.0 90.0 1.0

C.L.Pierotti, M.C.Tanzer, A.V.Jacobsen, J.M.Hildebrand, J.M.Garnier, P.Sharma, I.S.Lucet, A.D.Cowan, P.E.Czabotar, J.Silke, M.F.Van Delft, J.M.Murphy, G.L.Lessene. Necroptosis Can Be Potently Inhibited By Simultaneous Targeting of Multiple Effectors To Be Published.