Cobalt in PDB 5ikq: The Structure of Meclofenamic Acid Bound to Human Cyclooxygenase-2

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

The structure of The Structure of Meclofenamic Acid Bound to Human Cyclooxygenase-2, PDB code: 5ikq 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)	39.20 / 2.41
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	120.509, 134.053, 179.382, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 21.2

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

Chlorine

(Cl)

4 atoms

The binding sites of Cobalt atom in the The Structure of Meclofenamic Acid Bound to Human Cyclooxygenase-2 (pdb code 5ikq). 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 Meclofenamic Acid Bound to Human Cyclooxygenase-2, PDB code: 5ikq:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the The Structure of Meclofenamic 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 Meclofenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co609 b:78.4 occ:1.00 CO A:COH609 0.0 78.4 1.0 NC A:COH609 2.0 80.5 1.0 NA A:COH609 2.1 79.8 1.0 NB A:COH609 2.1 81.9 1.0 ND A:COH609 2.1 84.3 1.0 C4C A:COH609 3.0 80.3 1.0 C1D A:COH609 3.1 83.5 1.0 C1C A:COH609 3.1 79.5 1.0 C4A A:COH609 3.1 77.7 1.0 C1A A:COH609 3.1 81.0 1.0 C1B A:COH609 3.1 79.1 1.0 C4D A:COH609 3.1 82.7 1.0 C4B A:COH609 3.1 79.3 1.0 CHD A:COH609 3.4 81.8 1.0 CHB A:COH609 3.4 77.1 1.0 CHA A:COH609 3.5 81.6 1.0 CHC A:COH609 3.5 79.0 1.0 HD2 A:HIS388 3.7 71.5 1.0 HE21 A:GLN203 3.8 59.8 1.0 HE2 A:HIS388 3.8 75.0 1.0 HE2 A:HIS207 3.9 68.5 1.0 HG11 A:VAL447 4.2 51.4 1.0 NE2 A:GLN203 4.2 44.7 1.0 HE22 A:GLN203 4.3 59.8 1.0 C3C A:COH609 4.3 79.0 1.0 C2C A:COH609 4.3 78.7 1.0 CD2 A:HIS388 4.3 56.3 1.0 C2D A:COH609 4.3 80.1 1.0 HE1 A:HIS207 4.3 69.5 1.0 C3A A:COH609 4.3 78.3 1.0 C2A A:COH609 4.3 79.7 1.0 C3D A:COH609 4.3 79.3 1.0 C2B A:COH609 4.3 79.2 1.0 C3B A:COH609 4.3 78.0 1.0 HHD A:COH609 4.3 98.3 1.0 NE2 A:HIS388 4.4 57.5 1.0 HHB A:COH609 4.4 92.8 1.0 HHC A:COH609 4.4 95.0 1.0 HHA A:COH609 4.4 98.2 1.0 NE2 A:HIS207 4.5 50.8 1.0 HG3 A:GLN203 4.6 52.1 1.0 CE1 A:HIS207 4.8 50.8 1.0 CD A:GLN203 5.0 44.6 1.0

Cobalt binding site 2 out of 2 in the The Structure of Meclofenamic 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 Meclofenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co601 b:75.2 occ:1.00 CO B:COH601 0.0 75.2 1.0 NC B:COH601 2.0 81.5 1.0 NA B:COH601 2.1 84.1 1.0 NB B:COH601 2.1 83.8 1.0 ND B:COH601 2.1 81.4 1.0 C1C B:COH601 3.1 80.1 1.0 C4C B:COH601 3.1 80.5 1.0 C4B B:COH601 3.1 83.5 1.0 C1A B:COH601 3.1 83.0 1.0 C4A B:COH601 3.1 83.2 1.0 C1B B:COH601 3.1 82.3 1.0 C1D B:COH601 3.1 80.0 1.0 C4D B:COH601 3.1 81.2 1.0 HD2 B:HIS389 3.4 69.1 1.0 CHC B:COH601 3.4 81.9 1.0 CHD B:COH601 3.4 79.8 1.0 CHB B:COH601 3.4 81.8 1.0 HE2 B:HIS389 3.4 72.1 1.0 CHA B:COH601 3.5 81.5 1.0 CD2 B:HIS389 4.0 54.3 1.0 NE2 B:HIS389 4.0 54.9 1.0 HE1 B:HIS208 4.1 64.9 1.0 HG11 B:VAL448 4.2 45.9 1.0 HE2 B:HIS208 4.3 68.3 1.0 C3A B:COH601 4.3 82.4 1.0 C2A B:COH601 4.3 83.0 1.0 C2B B:COH601 4.3 83.1 1.0 C3B B:COH601 4.3 83.6 1.0 C2C B:COH601 4.3 78.7 1.0 C3C B:COH601 4.3 78.0 1.0 C2D B:COH601 4.3 81.1 1.0 C3D B:COH601 4.3 81.1 1.0 HHD B:COH601 4.4 96.0 1.0 HHC B:COH601 4.4 98.5 1.0 HHA B:COH601 4.4 98.1 1.0 HHB B:COH601 4.4 98.4 1.0 HE21 B:GLN204 4.4 61.3 1.0 HG3 B:GLN204 4.5 49.9 1.0 CE1 B:HIS208 4.8 45.5 1.0 NE2 B:GLN204 4.8 41.4 1.0 NE2 B:HIS208 4.8 46.2 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