Iron in PDB 3ln1: Structure of Celecoxib Bound at the Cox-2 Active Site

All present enzymatic activity of Structure of Celecoxib Bound at the Cox-2 Active Site:
1.14.99.1;

The structure of Structure of Celecoxib Bound at the Cox-2 Active Site, PDB code: 3ln1 was solved by J.R.Kiefer, R.G.Kurumbail, W.C.Stallings, J.L.Pawlitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.77 / 2.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	180.942, 135.377, 124.079, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 26.4

The structure of Structure of Celecoxib Bound at the Cox-2 Active Site also contains other interesting chemical elements:

Fluorine

(F)

12 atoms

The binding sites of Iron atom in the Structure of Celecoxib Bound at the Cox-2 Active Site (pdb code 3ln1). 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 Celecoxib Bound at the Cox-2 Active Site, PDB code: 3ln1:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of Celecoxib Bound at the Cox-2 Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Celecoxib Bound at the Cox-2 Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe605 b:39.6 occ:1.00 FE A:HEM605 0.0 39.6 1.0 ND A:HEM605 2.0 39.8 1.0 NA A:HEM605 2.0 39.8 1.0 NE2 A:HIS374 2.1 41.2 1.0 NC A:HEM605 2.1 39.9 1.0 NB A:HEM605 2.1 39.5 1.0 C1D A:HEM605 3.0 39.7 1.0 C4D A:HEM605 3.0 41.2 1.0 CD2 A:HIS374 3.0 40.9 1.0 C1A A:HEM605 3.0 42.4 1.0 CE1 A:HIS374 3.0 41.5 1.0 C4C A:HEM605 3.0 39.6 1.0 C4A A:HEM605 3.1 39.4 1.0 C1C A:HEM605 3.1 40.6 1.0 C1B A:HEM605 3.2 38.9 1.0 C4B A:HEM605 3.2 39.8 1.0 CHD A:HEM605 3.3 40.9 1.0 CHA A:HEM605 3.4 42.3 1.0 CHB A:HEM605 3.5 38.1 1.0 CHC A:HEM605 3.5 40.1 1.0 ND1 A:HIS374 4.1 40.6 1.0 CG A:HIS374 4.1 40.6 1.0 C2D A:HEM605 4.2 39.7 1.0 C3D A:HEM605 4.2 40.3 1.0 C2A A:HEM605 4.2 45.4 1.0 C3A A:HEM605 4.3 42.5 1.0 C3C A:HEM605 4.3 40.3 1.0 NE2 A:GLN189 4.3 37.6 1.0 C2C A:HEM605 4.3 41.0 1.0 C2B A:HEM605 4.4 38.6 1.0 C3B A:HEM605 4.4 39.9 1.0 NE2 A:HIS193 4.4 38.9 1.0 CE1 A:HIS193 4.7 39.1 1.0 CG1 A:VAL433 5.0 44.0 1.0

Iron binding site 2 out of 4 in the Structure of Celecoxib Bound at the Cox-2 Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Celecoxib Bound at the Cox-2 Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe605 b:43.5 occ:1.00 FE B:HEM605 0.0 43.5 1.0 ND B:HEM605 2.0 44.4 1.0 NA B:HEM605 2.0 43.6 1.0 NC B:HEM605 2.1 43.9 1.0 NB B:HEM605 2.1 44.3 1.0 NE2 B:HIS374 2.1 41.4 1.0 C1A B:HEM605 2.9 46.0 1.0 C4D B:HEM605 2.9 45.1 1.0 C4C B:HEM605 3.1 43.3 1.0 C1D B:HEM605 3.1 44.8 1.0 C1C B:HEM605 3.1 43.2 1.0 CE1 B:HIS374 3.1 41.5 1.0 C4A B:HEM605 3.1 45.1 1.0 CD2 B:HIS374 3.1 41.0 1.0 C4B B:HEM605 3.1 43.4 1.0 C1B B:HEM605 3.2 44.2 1.0 CHA B:HEM605 3.2 45.4 1.0 CHD B:HEM605 3.4 45.0 1.0 CHC B:HEM605 3.4 45.0 1.0 CHB B:HEM605 3.5 44.7 1.0 ND1 B:HIS374 4.2 40.9 1.0 C3D B:HEM605 4.2 45.3 1.0 C2A B:HEM605 4.2 49.0 1.0 CG B:HIS374 4.2 40.7 1.0 C2D B:HEM605 4.3 44.9 1.0 C3A B:HEM605 4.3 46.3 1.0 C3C B:HEM605 4.3 41.1 1.0 C2C B:HEM605 4.3 42.3 1.0 NE2 B:HIS193 4.3 39.3 1.0 C3B B:HEM605 4.3 43.3 1.0 NE2 B:GLN189 4.4 37.5 1.0 C2B B:HEM605 4.4 44.5 1.0 CE1 B:HIS193 4.6 39.1 1.0

Iron binding site 3 out of 4 in the Structure of Celecoxib Bound at the Cox-2 Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Celecoxib Bound at the Cox-2 Active Site within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe605 b:43.5 occ:1.00 FE C:HEM605 0.0 43.5 1.0 ND C:HEM605 1.9 43.3 1.0 NA C:HEM605 2.0 46.2 1.0 NE2 C:HIS374 2.0 41.5 1.0 NC C:HEM605 2.1 43.6 1.0 NB C:HEM605 2.1 43.8 1.0 CD2 C:HIS374 2.9 41.1 1.0 C1D C:HEM605 2.9 42.1 1.0 C4D C:HEM605 2.9 43.2 1.0 C1A C:HEM605 3.0 46.7 1.0 CE1 C:HIS374 3.0 41.7 1.0 C4C C:HEM605 3.0 42.2 1.0 C4A C:HEM605 3.1 45.6 1.0 C1C C:HEM605 3.2 42.1 1.0 C1B C:HEM605 3.2 42.8 1.0 C4B C:HEM605 3.2 43.2 1.0 CHD C:HEM605 3.3 43.0 1.0 CHA C:HEM605 3.3 43.8 1.0 CHB C:HEM605 3.5 43.7 1.0 CHC C:HEM605 3.6 42.3 1.0 CG C:HIS374 4.1 40.8 1.0 ND1 C:HIS374 4.1 40.7 1.0 C2D C:HEM605 4.2 42.1 1.0 C3D C:HEM605 4.2 43.5 1.0 C2A C:HEM605 4.2 49.4 1.0 C3A C:HEM605 4.3 47.1 1.0 C3C C:HEM605 4.3 39.6 1.0 C2C C:HEM605 4.3 41.4 1.0 C3B C:HEM605 4.4 42.6 1.0 C2B C:HEM605 4.4 42.5 1.0 NE2 C:GLN189 4.4 37.5 1.0 NE2 C:HIS193 4.5 38.9 1.0 CE1 C:HIS193 4.7 39.1 1.0 CG1 C:VAL433 4.9 44.2 1.0

Iron binding site 4 out of 4 in the Structure of Celecoxib Bound at the Cox-2 Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Celecoxib Bound at the Cox-2 Active Site within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe605 b:44.0 occ:1.00 FE D:HEM605 0.0 44.0 1.0 ND D:HEM605 2.0 44.4 1.0 NC D:HEM605 2.0 41.4 1.0 NA D:HEM605 2.1 45.0 1.0 NB D:HEM605 2.1 43.6 1.0 NE2 D:HIS374 2.2 41.2 1.0 C1D D:HEM605 2.9 46.0 1.0 C4D D:HEM605 3.0 45.7 1.0 C4C D:HEM605 3.0 41.7 1.0 C1A D:HEM605 3.0 47.6 1.0 C4A D:HEM605 3.1 45.4 1.0 C1C D:HEM605 3.1 40.1 1.0 C1B D:HEM605 3.1 43.8 1.0 CE1 D:HIS374 3.1 41.6 1.0 C4B D:HEM605 3.2 41.8 1.0 CD2 D:HIS374 3.2 40.9 1.0 CHD D:HEM605 3.3 43.7 1.0 CHA D:HEM605 3.4 46.8 1.0 CHB D:HEM605 3.5 44.4 1.0 CHC D:HEM605 3.5 40.7 1.0 C3D D:HEM605 4.2 47.4 1.0 C2D D:HEM605 4.2 46.5 1.0 ND1 D:HIS374 4.2 40.8 1.0 C3C D:HEM605 4.3 40.5 1.0 NE2 D:HIS193 4.3 39.5 1.0 C2A D:HEM605 4.3 50.1 1.0 C2C D:HEM605 4.3 40.6 1.0 CG D:HIS374 4.3 40.7 1.0 C3A D:HEM605 4.3 48.6 1.0 NE2 D:GLN189 4.3 37.5 1.0 C2B D:HEM605 4.4 43.8 1.0 C3B D:HEM605 4.4 42.8 1.0 CE1 D:HIS193 4.5 39.2 1.0 CG1 D:VAL433 5.0 44.0 1.0

J.L.Wang, D.Limburg, M.J.Graneto, J.Springer, J.R.Hamper, S.Liao, J.L.Pawlitz, R.G.Kurumbail, T.Maziasz, J.J.Talley, J.R.Kiefer, J.Carter. The Novel Benzopyran Class of Selective Cyclooxygenase-2 Inhibitors. Part 2: the Second Clinical Candidate Having A Shorter and Favorable Human Half-Life. Bioorg.Med.Chem.Lett. V. 20 7159 2010.
ISSN: ISSN 0960-894X
PubMed: 20709553
DOI: 10.1016/J.BMCL.2010.07.054