Iron in PDB 3rr3: Structure of (R)-Flurbiprofen Bound to Mcox-2

All present enzymatic activity of Structure of (R)-Flurbiprofen Bound to Mcox-2:
1.14.99.1;

The structure of Structure of (R)-Flurbiprofen Bound to Mcox-2, PDB code: 3rr3 was solved by K.C.Duggan, D.J.Hermanson, J.Musee, J.J.Prusakiewicz, J.Scheib, B.D.Carter, S.Banerjee, J.A.Oates, L.J.Marnett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 2.84
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	180.615, 134.549, 122.775, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 24.4

The structure of Structure of (R)-Flurbiprofen Bound to Mcox-2 also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Iron atom in the Structure of (R)-Flurbiprofen Bound to Mcox-2 (pdb code 3rr3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of (R)-Flurbiprofen Bound to Mcox-2, PDB code: 3rr3:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of (R)-Flurbiprofen Bound to Mcox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of (R)-Flurbiprofen Bound to Mcox-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe682 b:54.4 occ:1.00 FE A:HEM682 0.0 54.4 1.0 NA A:HEM682 2.0 56.7 1.0 NC A:HEM682 2.0 42.3 1.0 ND A:HEM682 2.1 62.1 1.0 NB A:HEM682 2.1 53.0 1.0 NE2 A:HIS388 2.4 43.0 1.0 C1A A:HEM682 3.0 62.4 1.0 C1C A:HEM682 3.1 43.7 1.0 C4C A:HEM682 3.1 41.3 1.0 C4A A:HEM682 3.1 54.6 1.0 C1D A:HEM682 3.1 57.9 1.0 C4D A:HEM682 3.1 64.4 1.0 C4B A:HEM682 3.1 48.0 1.0 CD2 A:HIS388 3.1 51.6 1.0 C1B A:HEM682 3.2 48.1 1.0 CHD A:HEM682 3.4 44.4 1.0 CHA A:HEM682 3.4 64.4 1.0 CHC A:HEM682 3.5 50.6 1.0 CHB A:HEM682 3.5 41.7 1.0 CE1 A:HIS388 3.5 56.4 1.0 NE2 A:GLN203 4.1 40.4 1.0 C2C A:HEM682 4.3 39.4 1.0 C2A A:HEM682 4.3 60.9 1.0 C3A A:HEM682 4.3 62.8 1.0 C3C A:HEM682 4.3 42.0 1.0 C2D A:HEM682 4.3 51.7 1.0 C3D A:HEM682 4.3 57.3 1.0 C3B A:HEM682 4.4 44.5 1.0 CG A:HIS388 4.4 46.5 1.0 C2B A:HEM682 4.4 41.6 1.0 ND1 A:HIS388 4.5 50.0 1.0 NE2 A:HIS207 4.6 63.7 1.0 CE1 A:HIS207 4.7 46.6 1.0 CD A:GLN203 4.9 48.3 1.0

Iron binding site 2 out of 4 in the Structure of (R)-Flurbiprofen Bound to Mcox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of (R)-Flurbiprofen Bound to Mcox-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe682 b:42.0 occ:1.00 FE B:HEM682 0.0 42.0 1.0 NC B:HEM682 2.0 43.3 1.0 ND B:HEM682 2.1 53.5 1.0 NB B:HEM682 2.1 46.0 1.0 NA B:HEM682 2.1 42.5 1.0 NE2 B:HIS388 2.6 40.9 1.0 C1C B:HEM682 3.0 41.6 1.0 C4B B:HEM682 3.0 41.0 1.0 C1A B:HEM682 3.1 53.0 1.0 C4D B:HEM682 3.1 51.0 1.0 C4C B:HEM682 3.1 49.5 1.0 C1D B:HEM682 3.1 43.5 1.0 C1B B:HEM682 3.1 54.1 1.0 C4A B:HEM682 3.1 50.9 1.0 CD2 B:HIS388 3.3 49.5 1.0 CHC B:HEM682 3.4 43.5 1.0 CHA B:HEM682 3.4 55.2 1.0 CHD B:HEM682 3.4 43.0 1.0 CHB B:HEM682 3.5 42.4 1.0 CE1 B:HIS388 3.7 52.6 1.0 O B:HOH648 3.7 58.8 1.0 NE2 B:GLN203 4.1 44.0 1.0 C2C B:HEM682 4.2 32.1 1.0 C3C B:HEM682 4.3 36.8 1.0 C3B B:HEM682 4.3 45.1 1.0 C2A B:HEM682 4.3 51.5 1.0 C3D B:HEM682 4.3 40.4 1.0 C2B B:HEM682 4.3 61.9 1.0 C2D B:HEM682 4.3 39.9 1.0 C3A B:HEM682 4.3 51.0 1.0 NE2 B:HIS207 4.4 64.7 1.0 CE1 B:HIS207 4.5 50.5 1.0 CG B:HIS388 4.5 50.2 1.0 ND1 B:HIS388 4.7 51.1 1.0 CD B:GLN203 4.9 49.9 1.0

Iron binding site 3 out of 4 in the Structure of (R)-Flurbiprofen Bound to Mcox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of (R)-Flurbiprofen Bound to Mcox-2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe682 b:50.1 occ:1.00 FE C:HEM682 0.0 50.1 1.0 NA C:HEM682 2.0 53.6 1.0 NC C:HEM682 2.1 52.0 1.0 ND C:HEM682 2.1 65.8 1.0 NB C:HEM682 2.1 57.6 1.0 NE2 C:HIS388 2.5 47.2 1.0 C1A C:HEM682 3.0 56.2 1.0 C4A C:HEM682 3.1 58.8 1.0 C4D C:HEM682 3.1 63.1 1.0 C1C C:HEM682 3.1 48.7 1.0 C4C C:HEM682 3.1 57.6 1.0 C1D C:HEM682 3.1 53.0 1.0 C4B C:HEM682 3.1 49.0 1.0 C1B C:HEM682 3.2 50.6 1.0 CD2 C:HIS388 3.2 54.0 1.0 CHA C:HEM682 3.4 64.2 1.0 CHC C:HEM682 3.4 52.1 1.0 CHD C:HEM682 3.5 48.3 1.0 CHB C:HEM682 3.5 44.0 1.0 CE1 C:HIS388 3.6 56.0 1.0 NE2 C:GLN203 4.1 47.4 1.0 C2A C:HEM682 4.2 55.3 1.0 C3A C:HEM682 4.3 58.0 1.0 C2C C:HEM682 4.3 50.6 1.0 C3C C:HEM682 4.3 57.8 1.0 C3D C:HEM682 4.3 61.4 1.0 C2D C:HEM682 4.3 59.6 1.0 C3B C:HEM682 4.3 45.8 1.0 C2B C:HEM682 4.4 54.0 1.0 CG C:HIS388 4.5 47.4 1.0 NE2 C:HIS207 4.5 61.8 1.0 ND1 C:HIS388 4.6 55.9 1.0 CE1 C:HIS207 4.7 51.0 1.0 O C:HOH642 4.9 47.5 1.0 CD C:GLN203 5.0 52.5 1.0

Iron binding site 4 out of 4 in the Structure of (R)-Flurbiprofen Bound to Mcox-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of (R)-Flurbiprofen Bound to Mcox-2 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe682 b:46.6 occ:1.00 FE D:HEM682 0.0 46.6 1.0 NA D:HEM682 2.0 45.6 1.0 NC D:HEM682 2.0 49.7 1.0 ND D:HEM682 2.1 47.8 1.0 NB D:HEM682 2.1 48.6 1.0 NE2 D:HIS388 2.5 40.6 1.0 C1A D:HEM682 3.1 56.6 1.0 C1D D:HEM682 3.1 43.0 1.0 C4B D:HEM682 3.1 51.5 1.0 C4C D:HEM682 3.1 45.1 1.0 C4D D:HEM682 3.1 47.2 1.0 C1C D:HEM682 3.1 46.8 1.0 C1B D:HEM682 3.1 49.1 1.0 C4A D:HEM682 3.1 43.0 1.0 CD2 D:HIS388 3.3 49.4 1.0 CHD D:HEM682 3.4 35.4 1.0 CHA D:HEM682 3.4 53.3 1.0 CHC D:HEM682 3.5 35.3 1.0 CHB D:HEM682 3.5 37.3 1.0 CE1 D:HIS388 3.6 52.8 1.0 NE2 D:GLN203 4.1 39.5 1.0 C3B D:HEM682 4.3 52.6 1.0 C2A D:HEM682 4.3 52.5 1.0 C2D D:HEM682 4.3 46.0 1.0 C2C D:HEM682 4.3 30.0 1.0 C3C D:HEM682 4.3 34.9 1.0 C2B D:HEM682 4.3 54.7 1.0 C3A D:HEM682 4.3 56.0 1.0 C3D D:HEM682 4.3 42.0 1.0 NE2 D:HIS207 4.4 57.0 1.0 CE1 D:HIS207 4.5 47.5 1.0 CG D:HIS388 4.5 51.8 1.0 ND1 D:HIS388 4.6 54.5 1.0 CD D:GLN203 4.9 49.8 1.0 CG D:GLN203 4.9 45.0 1.0

K.C.Duggan, D.J.Hermanson, J.Musee, J.J.Prusakiewicz, J.L.Scheib, B.D.Carter, S.Banerjee, J.A.Oates, L.J.Marnett. (R)-Profens Are Substrate-Selective Inhibitors of Endocannabinoid Oxygenation By Cox-2. Nat.Chem.Biol. V. 7 803 2011.
ISSN: ISSN 1552-4450
PubMed: 22053353
DOI: 10.1038/NCHEMBIO.663