Fluorine in PDB 7b33: MST3 in Complex with MRIA11

All present enzymatic activity of MST3 in Complex with MRIA11:
2.7.11.1;

The structure of MST3 in Complex with MRIA11, PDB code: 7b33 was solved by R.Tesch, M.Rak, A.C.Joerger, S.Knapp, Structural Genomics Consortium(Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.41 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	98.972, 58.954, 61.441, 90.00, 93.13, 90.00
R / Rfree (%)	18.1 / 20.8

The structure of MST3 in Complex with MRIA11 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the MST3 in Complex with MRIA11 (pdb code 7b33). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the MST3 in Complex with MRIA11, PDB code: 7b33:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the MST3 in Complex with MRIA11


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of MST3 in Complex with MRIA11 within 5.0Å range: probe atom residue distance (Å) B Occ A:F905 b:46.4 occ:1.00 F A:SQE905 0.0 46.4 1.0 C13 A:SQE905 1.3 45.2 1.0 F1 A:SQE905 2.1 50.5 1.0 C12 A:SQE905 2.4 35.6 1.0 N3 A:SQE905 2.8 30.1 1.0 OG A:SER46 3.2 61.7 1.0 CD2 A:PHE47 3.3 64.2 1.0 CD1 A:ILE67 3.4 42.0 1.0 CD A:LYS65 3.4 33.7 1.0 NZ A:LYS65 3.4 33.5 1.0 O A:SER46 3.5 48.0 1.0 C14 A:SQE905 3.5 36.9 1.0 CB A:PHE47 4.0 60.5 1.0 CE A:LYS65 4.0 30.3 1.0 C11 A:SQE905 4.1 28.3 1.0 CG A:PHE47 4.1 67.7 1.0 C A:SER46 4.2 53.3 1.0 CE2 A:PHE47 4.2 59.7 1.0 CD1 A:ILE109 4.2 30.9 1.0 CG1 A:ILE79 4.3 43.9 1.0 CB A:SER46 4.4 55.9 1.0 OE1 A:GLU82 4.4 59.4 1.0 CG1 A:ILE67 4.5 41.0 1.0 CG2 A:ILE79 4.5 38.7 1.0 C15 A:SQE905 4.6 38.0 1.0 CG A:LYS65 4.7 31.9 1.0 CB A:ILE79 4.8 39.9 1.0 C16 A:SQE905 4.8 34.0 1.0 O A:HOH1008 4.9 38.6 1.0 CA A:SER46 4.9 54.6 1.0 N A:PHE47 4.9 57.8 1.0 CA A:PHE47 5.0 61.5 1.0 CD1 A:ILE79 5.0 43.8 1.0

Fluorine binding site 2 out of 2 in the MST3 in Complex with MRIA11


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of MST3 in Complex with MRIA11 within 5.0Å range: probe atom residue distance (Å) B Occ A:F905 b:50.5 occ:1.00 F1 A:SQE905 0.0 50.5 1.0 C13 A:SQE905 1.4 45.2 1.0 F A:SQE905 2.1 46.4 1.0 C12 A:SQE905 2.4 35.6 1.0 C14 A:SQE905 2.8 36.9 1.0 CA A:ILE79 3.3 40.6 1.0 CD2 A:PHE47 3.4 64.2 1.0 OE1 A:GLU82 3.4 59.4 1.0 CG1 A:ILE79 3.5 43.9 1.0 N3 A:SQE905 3.5 30.1 1.0 CE2 A:PHE47 3.6 59.7 1.0 CB A:ILE79 3.7 39.9 1.0 CG2 A:ILE79 3.7 38.7 1.0 O A:ILE79 4.0 39.1 1.0 OG A:SER46 4.1 61.7 1.0 CB A:GLU82 4.1 41.6 1.0 C A:ILE79 4.1 40.6 1.0 N A:ILE79 4.2 39.2 1.0 C15 A:SQE905 4.2 38.0 1.0 O A:ASP78 4.2 46.1 1.0 CD A:GLU82 4.3 55.5 1.0 CG A:PHE47 4.5 67.7 1.0 C A:ASP78 4.5 46.0 1.0 CD1 A:ILE67 4.7 42.0 1.0 C11 A:SQE905 4.7 28.3 1.0 CD1 A:ILE79 4.8 43.8 1.0 CG A:GLU82 4.8 51.0 1.0 CZ A:PHE47 4.9 62.0 1.0 CD1 A:ILE109 4.9 30.9 1.0 C16 A:SQE905 5.0 34.0 1.0 CB A:PHE47 5.0 60.5 1.0

R.Tesch, M.Rak, A.C.Joerger, S.Knapp, Structural Genomics Consortium (Sgc). Structure-Based Design of Selective Salt-Inducible Kinase (Sik) Inhibitors To Be Published.