Fluorine in PDB 6v1j: Structure of Kpc-2 Bound to QPX7728 at 1.30 A

All present enzymatic activity of Structure of Kpc-2 Bound to QPX7728 at 1.30 A:
3.5.2.6;

The structure of Structure of Kpc-2 Bound to QPX7728 at 1.30 A, PDB code: 6v1j was solved by O.A.Pemberton, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.80 / 1.30
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.660, 59.990, 78.160, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 18

The binding sites of Fluorine atom in the Structure of Kpc-2 Bound to QPX7728 at 1.30 A (pdb code 6v1j). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structure of Kpc-2 Bound to QPX7728 at 1.30 A, PDB code: 6v1j:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structure of Kpc-2 Bound to QPX7728 at 1.30 A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Kpc-2 Bound to QPX7728 at 1.30 A within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:13.2 occ:1.00 F06 A:RM9301 0.0 13.2 1.0 C05 A:RM9301 1.3 11.3 1.0 C07 A:RM9301 2.4 12.7 1.0 C04 A:RM9301 2.4 9.6 1.0 C02 A:RM9301 2.8 9.5 1.0 O03 A:RM9301 2.9 10.1 1.0 O A:HOH619 3.0 28.1 1.0 O A:HOH519 3.1 13.7 1.0 OG1 A:THR237 3.4 8.8 1.0 C08 A:RM9301 3.6 10.8 1.0 C10 A:RM9301 3.6 9.2 1.0 O01 A:RM9301 3.7 11.3 1.0 CB A:THR237 4.0 9.1 1.0 C09 A:RM9301 4.1 9.4 1.0 O A:HOH655 4.2 53.0 1.0 NH2 A:ARG220 4.3 10.8 1.0 CZ2 A:TRP105 4.6 22.8 1.0 O A:HOH476 4.6 20.5 1.0 CG2 A:THR237 4.7 10.5 1.0 CH2 A:TRP105 4.7 23.2 1.0 O11 A:RM9301 4.8 8.6 1.0 CB A:THR216 5.0 10.5 1.0

Fluorine binding site 2 out of 2 in the Structure of Kpc-2 Bound to QPX7728 at 1.30 A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Kpc-2 Bound to QPX7728 at 1.30 A within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:23.2 occ:0.84 F06 A:QNA302 0.0 23.2 0.8 C05 A:QNA302 1.4 21.5 0.8 C07 A:QNA302 2.4 21.6 0.8 C04 A:QNA302 2.4 21.8 0.8 C02 A:QNA302 2.9 21.9 0.8 CD2 A:TYR129 3.2 13.3 1.0 CD1 A:ILE108 3.2 12.9 1.0 O01 A:QNA302 3.3 22.2 0.8 CE2 A:TYR129 3.4 13.6 1.0 CB A:PRO107 3.5 13.7 1.0 O A:HOH482 3.6 32.3 1.0 O03 A:QNA302 3.7 21.6 0.8 C08 A:QNA302 3.7 21.8 0.8 C10 A:QNA302 3.8 23.6 0.8 CG A:TYR129 4.0 12.6 1.0 CG1 A:ILE108 4.1 11.9 1.0 CG A:PRO107 4.1 14.4 1.0 C A:PRO107 4.2 12.4 1.0 C09 A:QNA302 4.2 23.1 0.8 O A:PRO107 4.2 14.1 1.0 CZ A:TYR129 4.3 14.9 1.0 CA A:PRO107 4.5 12.8 1.0 N A:ILE108 4.5 11.9 1.0 NZ A:LYS111 4.5 17.5 1.0 O A:HOH685 4.6 59.9 1.0 CE A:LYS111 4.6 17.3 1.0 CB A:TYR129 4.6 11.4 1.0 O A:HOH465 4.7 40.2 1.0 CD1 A:TYR129 4.8 13.1 1.0 O11 A:QNA302 4.9 26.2 0.8 CE1 A:TYR129 4.9 15.0 1.0 CA A:ILE108 4.9 11.2 1.0

S.J.Hecker, K.R.Reddy, O.Lomovskaya, D.C.Griffith, D.Rubio-Aparicio, K.Nelson, R.Tsivkovski, D.Sun, M.Sabet, Z.Tarazi, J.Parkinson, M.Totrov, S.H.Boyer, T.W.Glinka, O.A.Pemberton, Y.Chen, M.N.Dudley. Discovery of Cyclic Boronic Acid QPX7728, An Ultra-Broad-Spectrum Inhibitor of Serine and Metallo Beta-Lactamases. J.Med.Chem. 2020.
ISSN: ISSN 0022-2623
PubMed: 32150407
DOI: 10.1021/ACS.JMEDCHEM.9B01976