Fluorine in PDB 4x5z: Menin in Complex with Mi-136

The structure of Menin in Complex with Mi-136, PDB code: 4x5z was solved by J.Pollock, D.Borkin, T.Cierpicki, J.Grembecka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.95 / 1.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.013, 80.178, 124.887, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 20.8

The binding sites of Fluorine atom in the Menin in Complex with Mi-136 (pdb code 4x5z). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Menin in Complex with Mi-136, PDB code: 4x5z:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Menin in Complex with Mi-136


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Menin in Complex with Mi-136 within 5.0Å range: probe atom residue distance (Å) B Occ A:F605 b:15.2 occ:1.00 FAB A:3XY605 0.0 15.2 1.0 CBG A:3XY605 1.3 15.4 1.0 FAD A:3XY605 2.1 16.3 1.0 FAC A:3XY605 2.1 15.9 1.0 CAQ A:3XY605 2.4 14.0 1.0 C A:HIS181 3.0 13.3 1.0 CA A:HIS181 3.1 13.1 1.0 N A:HIS181 3.2 13.5 1.0 O A:HIS181 3.3 12.8 1.0 N A:ALA182 3.5 12.2 1.0 C A:ASP180 3.6 14.7 1.0 CB A:SER155 3.7 14.6 1.0 CAY A:3XY605 3.7 13.4 1.0 O A:HOH813 3.7 31.6 1.0 CB A:ALA182 3.9 12.1 1.0 O A:HOH783 3.9 22.2 1.0 O A:ASP180 4.0 14.2 1.0 OG A:SER155 4.2 13.0 1.0 CA A:ALA182 4.2 11.7 1.0 CA A:ASP180 4.5 14.5 1.0 O A:HOH776 4.6 23.6 1.0 CAK A:3XY605 4.6 13.9 1.0 CB A:HIS181 4.6 13.4 1.0 SAV A:3XY605 4.7 13.7 1.0 CA A:SER155 4.7 13.0 1.0

Fluorine binding site 2 out of 3 in the Menin in Complex with Mi-136


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Menin in Complex with Mi-136 within 5.0Å range: probe atom residue distance (Å) B Occ A:F605 b:15.9 occ:1.00 FAC A:3XY605 0.0 15.9 1.0 CBG A:3XY605 1.3 15.4 1.0 FAB A:3XY605 2.1 15.2 1.0 FAD A:3XY605 2.2 16.3 1.0 CAQ A:3XY605 2.3 14.0 1.0 CAY A:3XY605 2.8 13.4 1.0 SAV A:3XY605 3.1 13.7 1.0 CB A:SER155 3.3 14.6 1.0 CD2 A:LEU177 3.5 14.3 1.0 CE1 A:PHE238 3.5 13.8 1.0 OG A:SER155 3.7 13.0 1.0 CB A:ALA182 3.8 12.1 1.0 CAK A:3XY605 4.0 13.9 1.0 O A:HIS181 4.0 12.8 1.0 CZ A:PHE238 4.1 13.7 1.0 C A:HIS181 4.3 13.3 1.0 S A:DMS607 4.4 38.1 1.0 C4 A:3XY605 4.5 14.0 1.0 CD1 A:PHE238 4.6 12.7 1.0 N A:ALA182 4.6 12.2 1.0 C2 A:DMS607 4.6 33.5 1.0 CA A:ALA182 4.7 11.7 1.0 CA A:SER155 4.7 13.0 1.0 CG A:LEU177 4.8 14.1 1.0 C5 A:3XY605 4.8 14.0 1.0 N A:HIS181 4.9 13.5 1.0 CA A:HIS181 4.9 13.1 1.0 O A:HOH813 5.0 31.6 1.0

Fluorine binding site 3 out of 3 in the Menin in Complex with Mi-136


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Menin in Complex with Mi-136 within 5.0Å range: probe atom residue distance (Å) B Occ A:F605 b:16.3 occ:1.00 FAD A:3XY605 0.0 16.3 1.0 CBG A:3XY605 1.3 15.4 1.0 FAB A:3XY605 2.1 15.2 1.0 FAC A:3XY605 2.2 15.9 1.0 CAQ A:3XY605 2.3 14.0 1.0 CAY A:3XY605 2.8 13.4 1.0 O A:HOH813 3.0 31.6 1.0 O A:HOH863 3.3 40.4 1.0 CAK A:3XY605 3.3 13.9 1.0 OG A:SER155 3.5 13.0 1.0 CB A:SER155 3.7 14.6 1.0 S A:DMS607 3.8 38.1 1.0 O A:DMS607 3.8 44.2 1.0 O A:HOH776 3.9 23.6 1.0 SAV A:3XY605 4.0 13.7 1.0 C2 A:DMS607 4.1 33.5 1.0 C5 A:3XY605 4.4 14.0 1.0 C4 A:3XY605 4.7 14.0 1.0 N A:HIS181 4.7 13.5 1.0 C A:ASP180 4.8 14.7 1.0 CE1 A:PHE238 4.9 13.8 1.0

D.Borkin, S.He, H.Miao, K.Kempinska, J.Pollock, J.Chase, T.Purohit, B.Malik, T.Zhao, J.Wang, B.Wen, H.Zong, M.Jones, G.Danet-Desnoyers, M.L.Guzman, M.Talpaz, D.L.Bixby, D.Sun, J.L.Hess, A.G.Muntean, I.Maillard, T.Cierpicki, J.Grembecka. Pharmacologic Inhibition of the Menin-Mll Interaction Blocks Progression of Mll Leukemia in Vivo. Cancer Cell V. 27 589 2015.
ISSN: ISSN 1535-6108
PubMed: 25817203
DOI: 10.1016/J.CCELL.2015.02.016