Fluorine in PDB 3mvh: Crystal Structure of Akt-1-Inhibitor Complexes

All present enzymatic activity of Crystal Structure of Akt-1-Inhibitor Complexes:
2.7.11.1;

The structure of Crystal Structure of Akt-1-Inhibitor Complexes, PDB code: 3mvh was solved by J.Pandit, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.01
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.354, 55.261, 92.314, 90.00, 102.64, 90.00
R / Rfree (%)	17.8 / 23

The structure of Crystal Structure of Akt-1-Inhibitor Complexes also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Akt-1-Inhibitor Complexes (pdb code 3mvh). 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 Akt-1-Inhibitor Complexes, PDB code: 3mvh:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Akt-1-Inhibitor Complexes


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 Akt-1-Inhibitor Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:56.2 occ:1.00 F24 A:WFE999 0.0 56.2 1.0 C23 A:WFE999 1.3 54.2 1.0 C25 A:WFE999 2.3 54.6 1.0 C22 A:WFE999 2.4 55.7 1.0 N A:GLY162 3.4 54.6 1.0 CD2 A:LEU181 3.4 35.2 1.0 C26 A:WFE999 3.6 54.3 1.0 C21 A:WFE999 3.6 56.4 1.0 O A:GLY159 3.7 57.8 1.0 C A:GLY162 3.8 50.1 1.0 CB A:PHE161 3.9 59.2 1.0 CA A:GLY162 3.9 51.7 1.0 C A:PHE161 3.9 56.8 1.0 O A:GLY162 4.0 50.3 1.0 C20 A:WFE999 4.1 54.3 1.0 N A:LYS163 4.2 46.9 1.0 CA A:PHE161 4.3 58.5 1.0 CE A:LYS179 4.4 45.2 1.0 N A:PHE161 4.5 58.7 1.0 O A:PHE161 4.6 57.9 1.0 CG A:LYS179 4.6 35.8 1.0 C A:GLY159 4.6 58.0 1.0 F27 A:WFE999 4.7 54.1 1.0 CD1 A:PHE161 4.8 63.1 1.0 CG A:PHE161 4.8 60.8 1.0 CG A:LEU181 4.9 32.9 1.0 N A:GLY159 4.9 56.2 1.0 CA A:LYS163 5.0 44.6 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Akt-1-Inhibitor Complexes


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 Akt-1-Inhibitor Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:54.1 occ:1.00 F27 A:WFE999 0.0 54.1 1.0 C26 A:WFE999 1.3 54.3 1.0 C25 A:WFE999 2.3 54.6 1.0 C20 A:WFE999 2.4 54.3 1.0 O19 A:WFE999 2.5 55.7 1.0 C18 A:WFE999 2.7 52.1 1.0 N A:LYS158 3.0 50.2 1.0 C A:GLY157 3.1 46.7 1.0 CG2 A:VAL164 3.4 35.9 0.5 CG2 A:VAL164 3.4 38.5 0.5 O A:HOH1149 3.4 47.5 1.0 O A:GLY157 3.5 46.8 1.0 CA A:GLY157 3.5 45.5 1.0 CA A:LYS158 3.6 53.5 1.0 C23 A:WFE999 3.6 54.2 1.0 C21 A:WFE999 3.6 56.4 1.0 C A:LYS158 3.9 54.7 1.0 CG1 A:VAL164 3.9 37.8 0.5 N A:GLY159 3.9 56.2 1.0 N17 A:WFE999 3.9 45.7 1.0 N A:VAL164 4.0 39.9 0.5 N A:VAL164 4.1 40.3 0.5 C22 A:WFE999 4.1 55.7 1.0 CB A:VAL164 4.2 38.5 0.5 CB A:VAL164 4.2 37.4 0.5 C A:LYS163 4.3 41.6 1.0 CA A:LYS163 4.4 44.6 1.0 O A:LYS158 4.5 55.9 1.0 N A:GLY157 4.6 43.2 1.0 O A:GLY162 4.7 50.3 1.0 F24 A:WFE999 4.7 56.2 1.0 C13 A:WFE999 4.7 32.2 1.0 CA A:GLY159 4.7 57.0 1.0 CA A:VAL164 4.7 38.0 0.5 CA A:VAL164 4.8 38.9 0.5 C16 A:WFE999 4.9 36.9 1.0

K.D.Freeman-Cook, C.Autry, G.Borzillo, D.Gordon, E.Barbacci-Tobin, V.Bernardo, D.Briere, T.Clark, M.Corbett, J.Jakubczak, S.Kakar, E.Knauth, B.Lippa, M.J.Luzzio, M.Mansour, G.Martinelli, M.Marx, K.Nelson, J.Pandit, F.Rajamohan, S.Robinson, C.Subramanyam, L.Wei, M.Wythes, J.Morris. Design of Selective, Atp-Competitive Inhibitors of Akt. J.Med.Chem. V. 53 4615 2010.
ISSN: ISSN 0022-2623
PubMed: 20481595
DOI: 10.1021/JM1003842