Fluorine in PDB 4oty: Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2

All present enzymatic activity of Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2:
1.14.99.1;

The structure of Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2, PDB code: 4oty was solved by S.Xu, M.A.Windsor, S.Banerjee, L.J.Marnett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.12 / 2.35
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	122.663, 133.173, 181.546, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22.1

The structure of Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Fluorine atom in the Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2 (pdb code 4oty). 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 Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2, PDB code: 4oty:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2


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 Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F705 b:62.9 occ:1.00 FAD A:LUR705 0.0 62.9 1.0 CAP A:LUR705 1.3 54.1 1.0 CAG A:LUR705 2.4 64.1 1.0 CAT A:LUR705 2.5 49.2 1.0 NAM A:LUR705 2.9 60.1 1.0 CAS A:LUR705 3.2 51.8 1.0 CAJ A:LUR705 3.3 49.5 1.0 CG A:LEU352 3.6 48.4 1.0 CD2 A:LEU352 3.6 47.0 1.0 CAF A:LUR705 3.7 59.9 1.0 CAQ A:LUR705 3.8 52.6 1.0 CG2 A:VAL523 4.2 50.0 1.0 CAH A:LUR705 4.2 53.2 1.0 CB A:LEU352 4.2 45.2 1.0 CAR A:LUR705 4.2 49.5 1.0 N A:SER353 4.2 52.9 1.0 CA A:SER353 4.3 59.0 1.0 CAI A:LUR705 4.3 53.9 1.0 C A:LEU352 4.3 51.5 1.0 CG1 A:VAL523 4.4 37.8 1.0 CD2 A:PHE518 4.5 51.7 1.0 O A:LEU352 4.5 51.6 1.0 CE2 A:PHE518 4.6 55.0 1.0 CB A:VAL523 4.7 51.6 1.0 CB A:SER353 4.8 57.1 1.0 CD1 A:LEU352 4.8 45.1 1.0 CAL A:LUR705 4.9 38.8 1.0 CA A:VAL523 5.0 47.4 1.0 CA A:LEU352 5.0 47.7 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2


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 Lumiracoxib Bound to the Apo-Mouse- Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F705 b:64.4 occ:1.00 FAD B:LUR705 0.0 64.4 1.0 CAP B:LUR705 1.3 61.4 1.0 CAG B:LUR705 2.4 58.1 1.0 CAT B:LUR705 2.5 54.5 1.0 NAM B:LUR705 2.9 60.9 1.0 CAS B:LUR705 3.2 57.3 1.0 CAJ B:LUR705 3.2 58.1 1.0 CD2 B:LEU352 3.4 62.7 1.0 CG B:LEU352 3.4 68.7 1.0 CAF B:LUR705 3.7 42.3 1.0 CAQ B:LUR705 3.8 54.0 1.0 CB B:LEU352 4.1 64.4 1.0 CAH B:LUR705 4.2 46.3 1.0 CAI B:LUR705 4.2 54.7 1.0 CAR B:LUR705 4.3 57.4 1.0 CG2 B:VAL523 4.3 56.4 1.0 C B:LEU352 4.3 56.3 1.0 N B:SER353 4.3 49.8 1.0 CD2 B:PHE518 4.4 51.3 1.0 O B:LEU352 4.4 59.9 1.0 CA B:SER353 4.4 55.0 1.0 CE2 B:PHE518 4.4 47.3 1.0 CD1 B:LEU352 4.7 72.5 1.0 CG1 B:VAL523 4.7 52.6 1.0 CA B:LEU352 4.9 58.2 1.0 CB B:SER353 4.9 59.1 1.0 CAL B:LUR705 4.9 57.0 1.0 CB B:VAL523 4.9 52.4 1.0

M.A.Windsor, P.L.Valk, S.Xu, S.Banerjee, L.J.Marnett. Exploring the Molecular Determinants of Substrate-Selective Inhibition of Cyclooxygenase-2 By Lumiracoxib. Bioorg.Med.Chem.Lett. V. 23 5860 2013.
ISSN: ISSN 0960-894X
PubMed: 24060487
DOI: 10.1016/J.BMCL.2013.08.097