Fluorine in PDB 5tqh: IDH1 R132H Mutant in Complex with IDH889

All present enzymatic activity of IDH1 R132H Mutant in Complex with IDH889:
1.1.1.42;

The structure of IDH1 R132H Mutant in Complex with IDH889, PDB code: 5tqh was solved by X.Xie, R.Kulathila, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	112.62 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.731, 155.745, 163.048, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 22.5

The binding sites of Fluorine atom in the IDH1 R132H Mutant in Complex with IDH889 (pdb code 5tqh). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the IDH1 R132H Mutant in Complex with IDH889, PDB code: 5tqh:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the IDH1 R132H Mutant in Complex with IDH889


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of IDH1 R132H Mutant in Complex with IDH889 within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:55.5 occ:1.00 F7 A:7J2502 0.0 55.5 1.0 C4 A:7J2502 1.3 51.1 1.0 C3 A:7J2502 2.3 50.2 1.0 C5 A:7J2502 2.4 45.0 1.0 C8 A:7J2502 2.9 41.7 1.0 SD A:MET259 3.5 50.1 1.0 C2 A:7J2502 3.6 49.2 1.0 C6 A:7J2502 3.7 44.8 1.0 CG2 C:VAL281 3.7 39.5 1.0 CG1 C:VAL281 4.1 39.4 1.0 C1 A:7J2502 4.1 44.3 1.0 CG1 A:VAL255 4.5 33.6 1.0 CB C:VAL281 4.5 40.4 1.0 CG A:MET259 4.5 44.6 1.0 CE A:MET259 4.8 46.7 1.0

Fluorine binding site 2 out of 4 in the IDH1 R132H Mutant in Complex with IDH889


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of IDH1 R132H Mutant in Complex with IDH889 within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:44.8 occ:1.00 F7 B:7J2501 0.0 44.8 1.0 C4 B:7J2501 1.3 42.7 1.0 C3 B:7J2501 2.3 42.0 1.0 C5 B:7J2501 2.4 41.0 1.0 C8 B:7J2501 2.9 39.7 1.0 CG2 B:VAL255 3.6 37.9 1.0 C2 B:7J2501 3.6 40.7 1.0 C6 B:7J2501 3.6 38.0 1.0 CG1 B:VAL255 3.7 36.9 1.0 CH2 B:TRP267 4.0 37.6 1.0 CB B:VAL255 4.0 38.0 1.0 C1 B:7J2501 4.1 39.6 1.0 CA B:VAL255 4.3 35.3 1.0 CZ3 B:TRP267 4.5 37.0 1.0 O B:VAL255 5.0 41.0 1.0

Fluorine binding site 3 out of 4 in the IDH1 R132H Mutant in Complex with IDH889


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of IDH1 R132H Mutant in Complex with IDH889 within 5.0Å range: probe atom residue distance (Å) B Occ C:F501 b:53.9 occ:1.00 F7 C:7J2501 0.0 53.9 1.0 C4 C:7J2501 1.3 51.1 1.0 C3 C:7J2501 2.3 52.0 1.0 C5 C:7J2501 2.4 48.0 1.0 C8 C:7J2501 2.9 44.7 1.0 CG2 C:VAL255 3.4 42.2 1.0 C2 C:7J2501 3.6 53.6 1.0 CH2 C:TRP267 3.6 49.3 1.0 C6 C:7J2501 3.7 48.8 1.0 CG1 C:VAL255 3.7 41.6 1.0 CB C:VAL255 4.0 42.6 1.0 C1 C:7J2501 4.2 50.8 1.0 CZ3 C:TRP267 4.2 48.6 1.0 CA C:VAL255 4.3 40.7 1.0 CZ2 C:TRP267 4.7 49.4 1.0

Fluorine binding site 4 out of 4 in the IDH1 R132H Mutant in Complex with IDH889


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of IDH1 R132H Mutant in Complex with IDH889 within 5.0Å range: probe atom residue distance (Å) B Occ D:F501 b:62.0 occ:1.00 F7 D:7J2501 0.0 62.0 1.0 C4 D:7J2501 1.3 58.6 1.0 C3 D:7J2501 2.4 55.7 1.0 C5 D:7J2501 2.4 55.5 1.0 C8 D:7J2501 2.9 53.2 1.0 SD D:MET259 3.6 46.9 1.0 CG2 B:VAL281 3.6 35.8 1.0 C2 D:7J2501 3.6 52.3 1.0 C6 D:7J2501 3.7 51.4 1.0 CG1 B:VAL281 4.0 36.5 1.0 C1 D:7J2501 4.2 49.7 1.0 CB B:VAL281 4.4 36.8 1.0 CG D:MET259 4.4 43.5 1.0 CG1 D:VAL255 4.5 42.4 1.0 CE D:MET259 4.8 43.2 1.0

J.R.Levell, T.Caferro, G.Chenail, I.Dix, J.Dooley, B.Firestone, P.D.Fortin, J.Giraldes, T.Gould, J.D.Growney, M.D.Jones, R.Kulathila, F.Lin, G.Liu, A.Mueller, S.Van Der Plas, K.Slocum, T.Smith, R.Terranova, B.B.Toure, V.Tyagi, T.Wagner, X.Xie, M.Xu, F.S.Yang, L.X.Zhou, R.Pagliarini, Y.S.Cho. Optimization of 3-Pyrimidin-4-Yl-Oxazolidin-2-Ones As Allosteric and Mutant Specific Inhibitors of IDH1. Acs Med Chem Lett V. 8 151 2017.
ISSN: ISSN 1948-5875
PubMed: 28197303
DOI: 10.1021/ACSMEDCHEMLETT.6B00334