Fluorine in PDB 4rrw: Crystal Structure of Apo Murine Cyclooxygenase-2

All present enzymatic activity of Crystal Structure of Apo Murine Cyclooxygenase-2:
1.14.99.1;

The structure of Crystal Structure of Apo Murine Cyclooxygenase-2, PDB code: 4rrw was solved by S.Xu, A.L.Blobaum, S.Banerjee, L.J.Marnett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.12 / 2.57
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	215.711, 121.047, 135.111, 90.00, 123.20, 90.00
R / Rfree (%)	18.4 / 21.6

The structure of Crystal Structure of Apo Murine Cyclooxygenase-2 also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Fluorine atom in the Crystal Structure of Apo Murine Cyclooxygenase-2 (pdb code 4rrw). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of Apo Murine Cyclooxygenase-2, PDB code: 4rrw:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Crystal Structure of Apo Murine 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 Apo Murine Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F705 b:37.0 occ:1.00 FAD A:LUR705 0.0 37.0 1.0 CAP A:LUR705 1.3 38.4 1.0 CAG A:LUR705 2.4 41.2 1.0 CAT A:LUR705 2.5 39.3 1.0 NAM A:LUR705 2.9 41.3 1.0 CD1 A:LEU352 3.1 60.7 1.0 CAJ A:LUR705 3.2 39.9 1.0 CAS A:LUR705 3.2 38.8 1.0 CAF A:LUR705 3.6 42.3 1.0 CAQ A:LUR705 3.8 37.9 1.0 CG2 A:VAL523 4.0 39.5 1.0 CG1 A:VAL523 4.1 33.9 1.0 CG A:LEU352 4.1 54.9 1.0 CAH A:LUR705 4.2 39.6 1.0 N A:SER353 4.2 39.2 1.0 CAI A:LUR705 4.2 41.1 1.0 CA A:SER353 4.2 38.4 1.0 CAR A:LUR705 4.3 37.0 1.0 C A:LEU352 4.3 44.0 1.0 CD2 A:LEU352 4.3 56.6 1.0 O A:LEU352 4.3 46.0 1.0 CB A:LEU352 4.4 47.4 1.0 CB A:VAL523 4.5 38.2 1.0 CD2 A:PHE518 4.6 39.8 1.0 CE2 A:PHE518 4.6 39.1 1.0 O A:HOH920 4.6 49.8 1.0 CB A:SER353 4.7 35.5 1.0 CA A:VAL523 4.9 39.8 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Apo Murine 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 Apo Murine Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F705 b:50.1 occ:1.00 FAD B:LUR705 0.0 50.1 1.0 CAP B:LUR705 1.3 45.1 1.0 CAG B:LUR705 2.4 45.1 1.0 CAT B:LUR705 2.5 42.2 1.0 NAM B:LUR705 2.9 42.0 1.0 CD1 B:LEU352 3.1 63.1 1.0 CAJ B:LUR705 3.2 43.6 1.0 CAS B:LUR705 3.2 43.9 1.0 CAF B:LUR705 3.6 46.6 1.0 CAQ B:LUR705 3.8 41.1 1.0 CG2 B:VAL523 4.0 56.5 1.0 CG1 B:VAL523 4.0 53.3 1.0 CAH B:LUR705 4.2 42.3 1.0 CAI B:LUR705 4.2 39.8 1.0 CG B:LEU352 4.2 58.9 1.0 CA B:SER353 4.3 54.4 1.0 CAR B:LUR705 4.3 45.9 1.0 N B:SER353 4.3 55.9 1.0 C B:LEU352 4.4 59.8 1.0 CB B:VAL523 4.5 55.2 1.0 O B:LEU352 4.5 63.4 1.0 CD2 B:LEU352 4.5 59.3 1.0 CB B:LEU352 4.6 56.9 1.0 CD2 B:PHE518 4.6 45.2 1.0 CB B:SER353 4.7 54.4 1.0 CE2 B:PHE518 4.7 44.6 1.0 CA B:VAL523 4.8 52.6 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Apo Murine Cyclooxygenase-2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Apo Murine Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ C:F705 b:46.7 occ:1.00 FAD C:LUR705 0.0 46.7 1.0 CAP C:LUR705 1.3 42.5 1.0 CAG C:LUR705 2.4 41.3 1.0 CAT C:LUR705 2.5 41.2 1.0 NAM C:LUR705 2.9 40.7 1.0 CD1 C:LEU352 3.1 60.5 1.0 CAJ C:LUR705 3.2 34.2 1.0 CAS C:LUR705 3.2 36.3 1.0 CAF C:LUR705 3.7 41.2 1.0 CAQ C:LUR705 3.8 40.2 1.0 CG1 C:VAL523 4.0 41.4 1.0 CG2 C:VAL523 4.1 40.6 1.0 CG C:LEU352 4.2 54.6 1.0 CAH C:LUR705 4.2 40.3 1.0 CAI C:LUR705 4.2 36.8 1.0 CAR C:LUR705 4.3 35.7 1.0 N C:SER353 4.3 45.5 1.0 CA C:SER353 4.3 45.1 1.0 C C:LEU352 4.4 49.8 1.0 CD2 C:LEU352 4.4 50.5 1.0 CB C:LEU352 4.5 52.0 1.0 O C:LEU352 4.5 49.0 1.0 CB C:VAL523 4.6 43.6 1.0 CD2 C:PHE518 4.6 44.2 1.0 CE2 C:PHE518 4.6 44.2 1.0 CB C:SER353 4.7 42.3 1.0 CA C:VAL523 4.9 42.2 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Apo Murine Cyclooxygenase-2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Apo Murine Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ D:F705 b:47.8 occ:1.00 FAD D:LUR705 0.0 47.8 1.0 CAP D:LUR705 1.3 37.7 1.0 CAG D:LUR705 2.4 30.7 1.0 CAT D:LUR705 2.5 35.9 1.0 NAM D:LUR705 2.9 35.0 1.0 CAS D:LUR705 3.2 30.6 1.0 CAJ D:LUR705 3.3 31.6 1.0 CAF D:LUR705 3.7 34.0 1.0 CAQ D:LUR705 3.8 35.4 1.0 CD1 D:LEU352 3.9 38.8 1.0 CB D:LEU352 3.9 45.8 1.0 C D:LEU352 4.1 49.0 1.0 O D:LEU352 4.1 51.0 1.0 CG2 D:VAL523 4.1 45.5 1.0 CG1 D:VAL523 4.2 44.7 1.0 N D:SER353 4.2 49.6 1.0 CAH D:LUR705 4.2 36.9 1.0 CA D:SER353 4.3 48.9 1.0 CAI D:LUR705 4.3 34.6 1.0 CAR D:LUR705 4.3 31.9 1.0 CG D:LEU352 4.5 44.0 1.0 CD2 D:PHE518 4.6 45.5 1.0 CE2 D:PHE518 4.6 48.1 1.0 CB D:VAL523 4.6 45.4 1.0 CA D:LEU352 4.7 46.5 1.0 CB D:SER353 4.9 50.8 1.0 CA D:VAL523 4.9 43.0 1.0 CD2 D:LEU352 5.0 42.7 1.0

A.L.Blobaum, S.Xu, S.W.Rowlinson, K.C.Duggan, S.Banerjee, S.N.Kudalkar, W.R.Birmingham, K.Ghebreselasie, L.J.Marnett. Action at A Distance: Mutations of Peripheral Residues Transform Rapid Reversible Inhibitors to Slow, Tight Binders of Cyclooxygenase-2. J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M114.635987