Fluorine in PDB 1d3g: Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog

All present enzymatic activity of Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog:
1.3.3.1;

The structure of Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog, PDB code: 1d3g was solved by S.Liu, E.A.Neidhardt, T.H.Grossman, T.Ocain, J.Clardy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.610, 90.610, 122.410, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 18.8

The binding sites of Fluorine atom in the Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog (pdb code 1d3g). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog, PDB code: 1d3g:

Fluorine binding site 1 out of 1 in the Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Dihydroorotate Dehydrogenase Complexed with Brequinar Analog within 5.0Å range: probe atom residue distance (Å) B Occ A:F397 b:22.7 occ:1.00 F1 A:BRE397 0.0 22.7 1.0 C14 A:BRE397 1.2 21.1 1.0 C15 A:BRE397 2.3 19.0 1.0 C10 A:BRE397 2.3 18.5 1.0 CG1 A:VAL134 3.2 21.1 1.0 C11 A:BRE397 3.5 18.3 1.0 C6 A:BRE397 3.5 17.9 1.0 C7M A:FMN398 3.8 16.2 1.0 CG1 A:VAL143 4.0 15.7 1.0 C7 A:BRE397 4.0 17.7 1.0 CB A:PRO52 4.4 21.4 1.0 CB A:VAL134 4.5 20.5 1.0 O A:PRO52 4.6 20.6 1.0 CG2 A:VAL143 4.6 16.2 1.0 CG2 A:VAL134 4.7 22.8 1.0 OH A:TYR356 4.7 15.1 1.0 C4 A:BRE397 4.7 17.6 1.0 CG2 A:THR360 4.7 19.5 1.0 C A:PRO52 4.9 21.0 1.0 CB A:HIS56 4.9 16.8 1.0 CB A:VAL143 4.9 15.0 1.0 ND1 A:HIS56 5.0 18.3 1.0

S.Liu, E.A.Neidhardt, T.H.Grossman, T.Ocain, J.Clardy. Structures of Human Dihydroorotate Dehydrogenase in Complex with Antiproliferative Agents. Structure Fold.Des. V. 8 25 2000.
ISSN: ISSN 0969-2126
PubMed: 10673429
DOI: 10.1016/S0969-2126(00)00077-0