Fluorine in PDB 6uel: CPS1 Bound to Allosteric Inhibitor H3B-193

All present enzymatic activity of CPS1 Bound to Allosteric Inhibitor H3B-193:
6.3.4.16;

The structure of CPS1 Bound to Allosteric Inhibitor H3B-193, PDB code: 6uel was solved by N.A.Larsen, T.V.Nguyen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	139.03 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	99.587, 132.342, 142.443, 90.00, 102.57, 90.00
R / Rfree (%)	17.2 / 20.9

The structure of CPS1 Bound to Allosteric Inhibitor H3B-193 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Fluorine atom in the CPS1 Bound to Allosteric Inhibitor H3B-193 (pdb code 6uel). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the CPS1 Bound to Allosteric Inhibitor H3B-193, PDB code: 6uel:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the CPS1 Bound to Allosteric Inhibitor H3B-193


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of CPS1 Bound to Allosteric Inhibitor H3B-193 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1602 b:26.5 occ:1.00 F1 A:Q5A1602 0.0 26.5 1.0 C6 A:Q5A1602 1.3 23.2 1.0 C5 A:Q5A1602 2.3 23.4 1.0 C7 A:Q5A1602 2.3 20.5 1.0 CE1 A:PHE809 3.2 21.4 1.0 C4 A:Q5A1602 3.6 22.6 1.0 C8 A:Q5A1602 3.6 20.6 1.0 CG1 A:VAL664 3.6 20.1 1.0 CG1 A:VAL653 3.8 18.7 1.0 CE A:MET881 3.9 27.9 1.0 CD1 A:PHE809 3.9 21.6 1.0 C3 A:Q5A1602 4.1 23.5 1.0 CZ A:PHE809 4.1 21.7 1.0 CD1 A:ILE851 4.2 20.8 1.0 CB A:VAL664 4.4 20.4 1.0 CG2 A:VAL664 4.4 22.1 1.0 CB A:VAL653 4.4 17.4 1.0 CG2 A:VAL653 4.9 19.1 1.0

Fluorine binding site 2 out of 2 in the CPS1 Bound to Allosteric Inhibitor H3B-193


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of CPS1 Bound to Allosteric Inhibitor H3B-193 within 5.0Å range: probe atom residue distance (Å) B Occ B:F1602 b:25.0 occ:1.00 F1 B:Q5A1602 0.0 25.0 1.0 C6 B:Q5A1602 1.3 23.2 1.0 C7 B:Q5A1602 2.3 21.8 1.0 C5 B:Q5A1602 2.3 24.5 1.0 CE1 B:PHE809 3.2 20.8 1.0 C8 B:Q5A1602 3.5 22.5 1.0 CG1 B:VAL653 3.5 22.1 1.0 C4 B:Q5A1602 3.6 23.6 1.0 CG1 B:VAL664 3.6 21.6 1.0 CE B:MET881 3.9 22.7 1.0 CD1 B:PHE809 4.0 21.6 1.0 C3 B:Q5A1602 4.1 23.1 1.0 CZ B:PHE809 4.1 20.4 1.0 CD1 B:ILE851 4.3 18.7 1.0 CB B:VAL653 4.4 21.2 1.0 CB B:VAL664 4.4 21.2 1.0 CG2 B:VAL664 4.5 23.2 1.0 CG2 B:VAL653 4.9 21.5 1.0

S.Yao, T.V.Nguyen, A.Rolfe, A.A.Agrawal, J.Ke, S.Peng, F.Colombo, S.Yu, P.Bouchard, J.Wu, K.C.Huang, X.Bao, K.Omoto, A.Selvaraj, L.Yu, S.Ioannidis, F.H.Vaillancourt, P.Zhu, N.A.Larsen, D.M.Bolduc. Small Molecule Inhibition of CPS1 Activity Through An Allosteric Pocket. Cell Chem Biol 2020.
ISSN: ESSN 2451-9456
PubMed: 32017919
DOI: 10.1016/J.CHEMBIOL.2020.01.009