Cobalt in PDB 5ikv: The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2

All present enzymatic activity of The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2:
1.14.99.1;

The structure of The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2, PDB code: 5ikv was solved by B.J.Orlando, M.G.Malkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.01 / 2.51
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	126.918, 149.334, 184.766, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 22.4

The structure of The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2 also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Cobalt atom in the The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2 (pdb code 5ikv). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2, PDB code: 5ikv:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co602 b:62.8 occ:1.00 CO A:COH602 0.0 62.8 1.0 ND A:COH602 2.0 66.7 1.0 NC A:COH602 2.0 73.0 1.0 NA A:COH602 2.1 72.8 1.0 NB A:COH602 2.1 70.6 1.0 NE2 A:HIS388 2.1 48.2 1.0 C4D A:COH602 3.0 64.1 1.0 C1D A:COH602 3.0 68.7 1.0 C4C A:COH602 3.0 71.9 1.0 CD2 A:HIS388 3.0 48.2 1.0 C1C A:COH602 3.1 71.8 1.0 C1A A:COH602 3.1 71.5 1.0 C1B A:COH602 3.1 65.1 1.0 C4A A:COH602 3.1 69.7 1.0 C4B A:COH602 3.1 68.0 1.0 CE1 A:HIS388 3.2 48.2 1.0 HD2 A:HIS388 3.2 56.3 1.0 HE1 A:HIS388 3.4 56.4 1.0 CHD A:COH602 3.4 70.4 1.0 CHA A:COH602 3.4 67.4 1.0 CHB A:COH602 3.4 68.5 1.0 CHC A:COH602 3.4 68.5 1.0 HE21 A:GLN203 3.8 46.4 1.0 HG11 A:VAL447 4.1 50.9 1.0 CG A:HIS388 4.2 48.1 1.0 HE1 A:HIS207 4.2 47.1 1.0 ND1 A:HIS388 4.2 48.2 1.0 C3D A:COH602 4.2 63.8 1.0 HE2 A:HIS207 4.3 55.6 1.0 C2D A:COH602 4.3 66.0 1.0 C3C A:COH602 4.3 71.5 1.0 C2C A:COH602 4.3 72.5 1.0 C2B A:COH602 4.3 59.7 1.0 HHD A:COH602 4.3 84.5 1.0 HHB A:COH602 4.3 82.3 1.0 C2A A:COH602 4.3 73.2 1.0 C3B A:COH602 4.3 63.3 1.0 C3A A:COH602 4.3 65.9 1.0 NE2 A:GLN203 4.3 40.7 1.0 HHA A:COH602 4.4 81.0 1.0 HG3 A:GLN203 4.4 42.3 1.0 HHC A:COH602 4.4 82.3 1.0 HE22 A:GLN203 4.5 46.4 1.0 CE1 A:HIS207 4.8 39.1 1.0 NE2 A:HIS207 4.8 40.6 1.0 CG1 A:VAL447 5.0 43.8 1.0

Cobalt binding site 2 out of 2 in the The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co602 b:48.0 occ:1.00 CO B:COH602 0.0 48.0 1.0 NC B:COH602 2.0 58.0 1.0 ND B:COH602 2.0 72.8 1.0 NA B:COH602 2.1 76.5 1.0 NB B:COH602 2.1 65.2 1.0 NE2 B:HIS388 2.1 48.6 1.0 CD2 B:HIS388 3.0 48.7 1.0 C1C B:COH602 3.0 59.3 1.0 C1D B:COH602 3.0 72.9 1.0 C4D B:COH602 3.0 72.7 1.0 C4C B:COH602 3.0 64.5 1.0 C1A B:COH602 3.1 75.1 1.0 CE1 B:HIS388 3.1 48.8 1.0 C4B B:COH602 3.1 61.1 1.0 C1B B:COH602 3.1 60.5 1.0 C4A B:COH602 3.1 69.2 1.0 HD2 B:HIS388 3.2 58.2 1.0 HE1 B:HIS388 3.3 57.1 1.0 CHD B:COH602 3.4 70.2 1.0 CHC B:COH602 3.4 57.9 1.0 CHA B:COH602 3.4 71.1 1.0 CHB B:COH602 3.5 61.0 1.0 HE21 B:GLN203 3.8 42.2 1.0 HE1 B:HIS207 4.1 43.1 1.0 CG B:HIS388 4.1 48.8 1.0 ND1 B:HIS388 4.1 48.8 1.0 HG11 B:VAL447 4.2 47.7 1.0 C2C B:COH602 4.2 60.8 1.0 HG3 B:GLN203 4.2 40.1 1.0 C3D B:COH602 4.3 76.5 1.0 C3C B:COH602 4.3 59.7 1.0 NE2 B:GLN203 4.3 35.9 1.0 C2D B:COH602 4.3 75.1 1.0 C2A B:COH602 4.3 77.8 1.0 C2B B:COH602 4.3 58.9 1.0 C3B B:COH602 4.3 58.3 1.0 HHD B:COH602 4.3 84.3 1.0 C3A B:COH602 4.4 68.7 1.0 HHB B:COH602 4.4 73.3 1.0 HHC B:COH602 4.4 69.5 1.0 HHA B:COH602 4.4 85.4 1.0 HE22 B:GLN203 4.5 42.2 1.0 NE2 B:HIS207 4.6 32.4 1.0 CE1 B:HIS207 4.7 33.0 1.0 HD1 B:HIS388 4.9 55.6 1.0 CD B:GLN203 4.9 35.4 1.0 HD11 B:LEU391 5.0 57.7 1.0

B.J.Orlando, M.G.Malkowski. Substrate-Selective Inhibition of Cyclooxygeanse-2 By Fenamic Acid Derivatives Is Dependent on Peroxide Tone. J.Biol.Chem. V. 291 15069 2016.
ISSN: ESSN 1083-351X
PubMed: 27226593
DOI: 10.1074/JBC.M116.725713