Fluorine in PDB 6n83: Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037

Enzymatic activity of 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;

Protein crystallography data

The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037, PDB code: 6n83 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) 78.67 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 111.080, 111.080, 76.730, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 21.7

Other elements in 6n83:

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

Chlorine (Cl) 3 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037 (pdb code 6n83). 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 Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Yf-02037, PDB code: 6n83:

Fluorine binding site 1 out of 1 in 6n83

Go back to Fluorine Binding Sites List in 6n83
Fluorine binding site 1 out of 1 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:F401

b:0.3
occ:1.00
 FBD F:YL6401 0.0 0.3 1.0
CAZ F:YL6401 1.4 0.2 1.0
CAY F:YL6401 2.4 92.5 1.0
CBA F:YL6401 2.4 92.5 1.0
NE2 F:GLN242 2.5 68.7 1.0
CD1 F:PHE239 3.2 67.9 1.0
CD F:GLN242 3.6 70.7 1.0
O F:ILE348 3.6 76.4 1.0
CB F:ILE348 3.6 72.8 1.0
CAX F:YL6401 3.7 91.2 1.0
CBB F:YL6401 3.7 92.2 1.0
CA F:PHE239 3.7 60.8 1.0
O F:PHE239 3.9 64.2 1.0
CE1 F:PHE239 4.0 68.7 1.0
CA F:ILE348 4.0 71.9 1.0
CG F:GLN242 4.0 70.8 1.0
CB F:GLN242 4.0 67.2 1.0
CG F:PHE239 4.0 64.2 1.0
CB F:PHE239 4.1 61.1 1.0
CBC F:YL6401 4.2 81.9 1.0
C F:ILE348 4.3 73.0 1.0
CG2 F:ILE348 4.3 70.0 1.0
C F:PHE239 4.3 61.2 1.0
CE2 F:PHE238 4.4 66.1 1.0
OE1 F:GLN242 4.6 77.3 1.0
CG1 F:ILE348 4.7 71.7 1.0
CD2 F:PHE238 4.7 64.7 1.0
CAV F:YL6401 4.8 90.8 1.0
N F:PHE239 4.8 56.3 1.0
O F:PHE238 4.9 59.1 1.0

Reference:

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
Page generated: Sun Dec 13 12:59:32 2020

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