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Fluorine in PDB 4rrz: Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib

Enzymatic activity of Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib

All present enzymatic activity of Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib:
1.14.99.1;

Protein crystallography data

The structure of Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib, PDB code: 4rrz 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

Other elements in 4rrz:

The structure of Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib (pdb code 4rrz). 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 H90W Cyclooxygenase-2 Complexed with Lumiracoxib, PDB code: 4rrz:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 4rrz

Go back to Fluorine Binding Sites List in 4rrz
Fluorine binding site 1 out of 4 in the Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib


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 H90W Cyclooxygenase-2 Complexed with Lumiracoxib 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 4rrz

Go back to Fluorine Binding Sites List in 4rrz
Fluorine binding site 2 out of 4 in the Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib


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 H90W Cyclooxygenase-2 Complexed with Lumiracoxib 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 4rrz

Go back to Fluorine Binding Sites List in 4rrz
Fluorine binding site 3 out of 4 in the Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib


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 H90W Cyclooxygenase-2 Complexed with Lumiracoxib 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 4rrz

Go back to Fluorine Binding Sites List in 4rrz
Fluorine binding site 4 out of 4 in the Crystal Structure of Apo Murine H90W Cyclooxygenase-2 Complexed with Lumiracoxib


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 H90W Cyclooxygenase-2 Complexed with Lumiracoxib 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

Reference:

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
Page generated: Tue Jul 15 00:41:16 2025

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