Fluorine in PDB 6n82: Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037

All present enzymatic activity of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037:
2.5.1.1; 2.5.1.10;

The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037, PDB code: 6n82 was solved by J.Park, M.A.Schilling, A.M.Berghuis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.43 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.920, 110.920, 77.530, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 20.4

The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037 also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Fluorine atom in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037 (pdb code 6n82). 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 Fpps in Complex with An Allosteric Inhibitor Yf-02037, PDB code: 6n82:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037


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 Fpps in Complex with An Allosteric Inhibitor Yf-02037 within 5.0Å range: probe atom residue distance (Å) B Occ F:F402 b:0.0 occ:1.00 FBA F:YF7402 0.0 0.0 1.0 CAY F:YF7402 1.3 0.2 1.0 CAZ F:YF7402 2.3 0.1 1.0 CAX F:YF7402 2.4 0.2 1.0 O F:HOH533 2.7 60.2 1.0 CAU F:YF7402 3.6 0.4 1.0 CAW F:YF7402 3.6 0.8 1.0 CE1 F:PHE239 3.7 64.2 1.0 OD1 F:ASP243 3.8 76.5 1.0 CB F:ASP243 3.8 66.1 1.0 CG F:ASP243 3.9 72.2 1.0 CA F:ASP243 4.1 66.8 1.0 CAV F:YF7402 4.1 0.3 1.0 CZ F:PHE239 4.2 63.3 1.0 CD1 F:PHE239 4.2 64.1 1.0 N F:ASP243 4.5 62.1 1.0 O F:PHE239 4.5 55.2 1.0 C4 F:YF7402 4.6 0.3 1.0 NE2 F:GLN242 4.6 65.8 1.0 C5 F:YF7402 4.7 0.9 1.0 OD2 F:ASP243 4.7 81.2 1.0 CD1 F:LEU246 4.7 76.5 1.0 CAT F:YF7402 4.7 0.6 1.0 N3 F:YF7402 4.7 0.9 1.0 NAR F:YF7402 4.9 0.9 1.0 C6 F:YF7402 4.9 94.0 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037


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 Fpps in Complex with An Allosteric Inhibitor Yf-02037 within 5.0Å range: probe atom residue distance (Å) B Occ F:F403 b:0.6 occ:1.00 FBA F:YF7403 0.0 0.6 1.0 CAY F:YF7403 1.3 0.1 1.0 CAZ F:YF7403 2.3 0.7 1.0 CAX F:YF7403 2.3 0.6 1.0 CAU F:YF7403 3.5 0.7 1.0 CAW F:YF7403 3.6 0.2 1.0 CG F:GLU319 3.8 84.6 1.0 CA F:GLU319 3.8 77.8 1.0 CAV F:YF7403 4.0 0.9 1.0 N F:GLU319 4.2 71.7 1.0 CB F:GLU319 4.3 80.3 1.0 O F:GLU318 4.5 68.6 1.0 C F:GLU318 4.5 72.3 1.0 CB F:TYR322 4.5 74.5 1.0 CG F:GLU318 4.6 77.9 1.0 CAT F:YF7403 4.6 0.2 1.0 CG F:TYR322 4.8 79.8 1.0 CD2 F:TYR322 4.9 85.3 1.0

Y.Feng, J.Park, S.G.Li, R.Boutin, P.Viereck, M.A.Schilling, A.M.Berghuis, Y.S.Tsantrizos. Chirality-Driven Mode of Binding of Alpha-Aminophosphonic Acid-Based Allosteric Inhibitors of the Human Farnesyl Pyrophosphate Synthase (Hfpps). J.Med.Chem. V. 62 9691 2019.
ISSN: ISSN 0022-2623
PubMed: 31577901
DOI: 10.1021/ACS.JMEDCHEM.9B01104