Fluorine in PDB 5de1: Crystal Structure of Human IDH1 in Complex with GSK321A

All present enzymatic activity of Crystal Structure of Human IDH1 in Complex with GSK321A:
1.1.1.42;

The structure of Crystal Structure of Human IDH1 in Complex with GSK321A, PDB code: 5de1 was solved by N.O.Concha, A.Smallwood, H.Qi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 2.25
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	82.726, 82.726, 303.639, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 25.8

The binding sites of Fluorine atom in the Crystal Structure of Human IDH1 in Complex with GSK321A (pdb code 5de1). 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 Human IDH1 in Complex with GSK321A, PDB code: 5de1:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Human IDH1 in Complex with GSK321A


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 Human IDH1 in Complex with GSK321A within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:66.2 occ:1.00 F A:59D502 0.0 66.2 1.0 C14 A:59D502 1.3 65.3 1.0 C13 A:59D502 2.3 65.3 1.0 C15 A:59D502 2.4 64.9 1.0 CZ3 A:TRP267 3.6 51.2 1.0 C12 A:59D502 3.6 64.4 1.0 C16 A:59D502 3.6 64.7 1.0 CH2 A:TRP267 3.6 51.1 1.0 C11 A:59D502 4.1 63.8 1.0 OG B:SER280 4.3 76.1 1.0 CG1 A:VAL255 4.4 68.7 1.0 SD A:MET259 4.4 72.3 1.0 CB A:VAL255 4.6 69.3 1.0 CE3 A:TRP267 4.8 50.7 1.0 CA A:VAL255 4.8 68.9 1.0 CZ2 A:TRP267 4.9 50.9 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Human IDH1 in Complex with GSK321A


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 Human IDH1 in Complex with GSK321A within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:62.7 occ:1.00 F B:59D502 0.0 62.7 1.0 C14 B:59D502 1.3 61.4 1.0 C15 B:59D502 2.3 60.2 1.0 C13 B:59D502 2.4 60.0 1.0 CH2 B:TRP267 3.5 52.0 1.0 CZ3 B:TRP267 3.6 51.4 1.0 C16 B:59D502 3.6 60.2 1.0 C12 B:59D502 3.6 59.6 1.0 C11 B:59D502 4.1 58.8 1.0 CG1 B:VAL255 4.2 71.3 1.0 CB B:VAL255 4.6 72.2 1.0 CB B:ALA258 4.7 70.4 1.0 CZ2 B:TRP267 4.8 51.5 1.0 CA B:VAL255 4.8 71.5 1.0 CE3 B:TRP267 4.9 50.9 1.0 SD B:MET259 4.9 77.9 1.0

U.C.Okoye-Okafor, B.Bartholdy, J.Cartier, E.N.Gao, B.Pietrak, A.R.Rendina, C.Rominger, C.Quinn, A.Smallwood, K.J.Wiggall, A.J.Reif, S.J.Schmidt, H.Qi, H.Zhao, G.Joberty, M.Faelth-Savitski, M.Bantscheff, G.Drewes, C.Duraiswami, P.Brady, A.Groy, S.R.Narayanagari, I.Antony-Debre, K.Mitchell, H.R.Wang, Y.R.Kao, M.Christopeit, L.Carvajal, L.Barreyro, E.Paietta, H.Makishima, B.Will, N.Concha, N.D.Adams, B.Schwartz, M.T.Mccabe, J.Maciejewski, A.Verma, U.Steidl. New IDH1 Mutant Inhibitors For Treatment of Acute Myeloid Leukemia. Nat.Chem.Biol. V. 11 878 2015.
ISSN: ESSN 1552-4469
PubMed: 26436839
DOI: 10.1038/NCHEMBIO.1930