Fluorine in PDB 3itz: Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor

All present enzymatic activity of Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor:
2.7.11.24;

The structure of Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor, PDB code: 3itz was solved by C.Mohr, S.Jordan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.94 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.245, 87.847, 121.258, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 24.9

The structure of Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor (pdb code 3itz). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor, PDB code: 3itz:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor


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 P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:23.1 occ:1.00 F1 A:P66401 0.0 23.1 1.0 C5 A:P66401 1.3 21.6 1.0 C8 A:P66401 2.4 22.2 1.0 C4 A:P66401 2.4 21.1 1.0 N3 A:P66401 2.8 21.1 1.0 CB A:ALA157 3.2 18.1 1.0 C1 A:P66401 3.3 21.1 1.0 N2 A:P66401 3.4 20.1 1.0 C6 A:P66401 3.6 21.8 1.0 C9 A:P66401 3.6 21.8 1.0 C11 A:P66401 3.8 20.7 1.0 CB A:MET109 3.8 16.6 1.0 CD1 A:LEU167 4.0 17.6 1.0 CA A:ALA157 4.1 17.8 1.0 C10 A:P66401 4.1 22.4 1.0 C3 A:P66401 4.2 20.5 1.0 C2 A:P66401 4.2 20.9 1.0 O A:ALA111 4.3 21.6 1.0 C A:ALA111 4.4 21.4 1.0 OH A:TYR35 4.5 33.7 1.0 CG A:MET109 4.6 18.2 1.0 CZ A:TYR35 4.6 32.9 1.0 N A:ASP112 4.6 22.4 1.0 O A:MET109 4.6 16.2 1.0 C A:MET109 4.7 16.4 1.0 CA A:MET109 4.7 16.4 1.0 F2 A:P66401 4.7 22.3 1.0 CE1 A:TYR35 4.9 32.7 1.0 N A:ALA111 4.9 19.4 1.0 CA A:ALA111 4.9 20.6 1.0 N6 A:P66401 4.9 21.9 1.0 CD2 A:LEU167 5.0 16.3 1.0 CG A:LEU167 5.0 16.0 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor


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 P38A Mitogen-Activated Protein Kinase in Complex with A Pyrazolopyridazine Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:22.3 occ:1.00 F2 A:P66401 0.0 22.3 1.0 C6 A:P66401 1.3 21.8 1.0 C10 A:P66401 2.4 22.4 1.0 C4 A:P66401 2.4 21.1 1.0 N3 A:P66401 2.7 21.1 1.0 CD1 A:LEU108 3.1 14.6 1.0 N2 A:P66401 3.3 20.1 1.0 C1 A:P66401 3.4 21.1 1.0 C9 A:P66401 3.6 21.8 1.0 C5 A:P66401 3.6 21.6 1.0 CG2 A:VAL30 3.7 29.4 1.0 C11 A:P66401 4.0 20.7 1.0 C8 A:P66401 4.1 22.2 1.0 O A:MET109 4.1 16.2 1.0 CB A:VAL30 4.1 29.2 1.0 C3 A:P66401 4.2 20.5 1.0 C2 A:P66401 4.3 20.9 1.0 O A:HOH443 4.3 14.8 1.0 CG A:LEU108 4.3 14.6 1.0 CB A:ALA51 4.5 13.8 1.0 CG1 A:VAL30 4.6 30.3 1.0 F1 A:P66401 4.7 23.1 1.0 CE2 A:TYR35 4.8 32.8 1.0 N A:MET109 4.8 16.0 1.0 CG1 A:VAL38 4.9 22.6 1.0 CD2 A:TYR35 4.9 31.8 1.0

R.P.Wurz, L.H.Pettus, B.Henkle, L.Sherman, M.Plant, K.Miner, H.J.Mcbride, L.M.Wong, C.J.Saris, M.R.Lee, S.Chmait, C.Mohr, F.Hsieh, A.S.Tasker. Part 2: Structure-Activity Relationship (Sar) Investigations of Fused Pyrazoles As Potent, Selective and Orally Available Inhibitors of P38ALPHA Mitogen-Activated Protein Kinase. Bioorg.Med.Chem.Lett. V. 20 1680 2010.
ISSN: ISSN 0960-894X
PubMed: 20138761
DOI: 10.1016/J.BMCL.2010.01.059