Fluorine in PDB 8p3c: Full Length Structure of Bpmip with Bound Inhibitor NJS227.

All present enzymatic activity of Full Length Structure of Bpmip with Bound Inhibitor NJS227.:
5.2.1.8;

The structure of Full Length Structure of Bpmip with Bound Inhibitor NJS227., PDB code: 8p3c was solved by J.J.Whittaker, A.Guskov, B.Goretzki, U.A.Hellmich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.21 / 2.02
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.608, 77.608, 52.995, 90, 90, 120
R / Rfree (%)	19.4 / 23.5

The binding sites of Fluorine atom in the Full Length Structure of Bpmip with Bound Inhibitor NJS227. (pdb code 8p3c). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Full Length Structure of Bpmip with Bound Inhibitor NJS227., PDB code: 8p3c:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Full Length Structure of Bpmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Full Length Structure of Bpmip with Bound Inhibitor NJS227. within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:34.9 occ:1.00 F1 B:WRX201 0.0 34.9 1.0 C1 B:WRX201 1.4 30.2 1.0 C2 B:WRX201 2.3 27.8 1.0 C28 B:WRX201 2.3 29.6 1.0 CB B:VAL97 3.3 44.6 1.0 CG1 B:VAL97 3.5 44.9 1.0 C3 B:WRX201 3.6 26.8 1.0 C27 B:WRX201 3.6 29.4 1.0 O B:PHE43 3.7 30.0 1.0 CG2 B:VAL97 3.7 50.1 1.0 C4 B:WRX201 4.1 25.5 1.0 CB B:PHE43 4.2 30.0 1.0 C B:PHE43 4.5 30.0 1.0 O B:ALA94 4.6 33.6 1.0 CA B:VAL97 4.6 39.0 1.0 CD1 B:PHE43 4.7 30.0 1.0 CG1 B:ILE98 4.7 33.1 1.0 CA B:PHE43 4.8 30.0 1.0 N B:ILE98 4.8 34.8 1.0 CG B:PHE43 4.8 30.0 1.0 C B:VAL97 5.0 42.4 1.0 CD1 B:ILE98 5.0 35.0 1.0

Fluorine binding site 2 out of 2 in the Full Length Structure of Bpmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Full Length Structure of Bpmip with Bound Inhibitor NJS227. within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:36.2 occ:1.00 F2 B:WRX201 0.0 36.2 1.0 C13 B:WRX201 1.4 35.1 1.0 C14 B:WRX201 2.3 34.6 1.0 C12 B:WRX201 2.3 33.2 1.0 C27 B:WRX201 3.5 29.4 1.0 C15 B:WRX201 3.6 32.3 1.0 C11 B:WRX201 3.6 27.0 1.0 C4 B:WRX201 3.9 25.5 1.0 C5 B:WRX201 4.0 27.0 1.0 C28 B:WRX201 4.1 29.6 1.0 C10 B:WRX201 4.1 28.5 1.0 C3 B:WRX201 4.8 26.8 1.0 OD2 B:ASP44 4.9 48.4 1.0 C1 B:WRX201 4.9 30.2 1.0

J.J.Whittaker, A.Guskov, B.Goretzki, U.A.Hellmich. Structural Dynamics of Macrophage Infectivity Potentiator Proteins (Mips) Are Differentially Modulated By Inhibitors and Appendage Domains To Be Published.