Cobalt in PDB 5ikr: The Structure of Mefenamic Acid Bound to Human Cyclooxygenase-2

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

The structure of The Structure of Mefenamic Acid Bound to Human Cyclooxygenase-2, PDB code: 5ikr 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)	20.00 / 2.34
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	127.672, 149.694, 188.391, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 21.1

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

Cobalt binding site 1 out of 2 in the The Structure of Mefenamic 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 Mefenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co602 b:51.4 occ:1.00 CO A:COH602 0.0 51.4 1.0 NC A:COH602 2.0 46.8 1.0 NA A:COH602 2.1 61.1 1.0 NB A:COH602 2.1 54.2 1.0 ND A:COH602 2.1 47.5 1.0 NE2 A:HIS388 2.1 39.6 1.0 C1C A:COH602 3.0 46.2 1.0 C4C A:COH602 3.0 45.9 1.0 C1B A:COH602 3.1 55.1 1.0 C4A A:COH602 3.1 60.0 1.0 CD2 A:HIS388 3.1 40.4 1.0 C1A A:COH602 3.1 58.5 1.0 C4B A:COH602 3.1 50.5 1.0 C1D A:COH602 3.1 45.3 1.0 CE1 A:HIS388 3.1 39.7 1.0 C4D A:COH602 3.1 49.7 1.0 HD2 A:HIS388 3.2 57.3 1.0 HE1 A:HIS388 3.3 57.2 1.0 CHD A:COH602 3.4 44.8 1.0 CHB A:COH602 3.4 57.1 1.0 CHC A:COH602 3.4 46.7 1.0 CHA A:COH602 3.5 53.5 1.0 HE21 A:GLN203 3.6 42.5 1.0 HE2 A:HIS207 3.9 46.4 1.0 NE2 A:GLN203 4.1 27.1 1.0 HG11 A:VAL447 4.1 50.5 1.0 ND1 A:HIS388 4.2 40.6 1.0 CG A:HIS388 4.2 40.9 1.0 HE1 A:HIS207 4.2 43.0 1.0 C2C A:COH602 4.3 44.1 1.0 C3C A:COH602 4.3 45.9 1.0 C2B A:COH602 4.3 53.1 1.0 HE22 A:GLN203 4.3 42.5 1.0 C3B A:COH602 4.3 51.7 1.0 C3A A:COH602 4.3 59.8 1.0 HG3 A:GLN203 4.3 28.0 1.0 C2A A:COH602 4.3 59.7 1.0 HHB A:COH602 4.3 69.1 1.0 C2D A:COH602 4.3 44.7 1.0 C3D A:COH602 4.4 48.2 1.0 HHD A:COH602 4.4 54.2 1.0 HHC A:COH602 4.4 56.6 1.0 HHA A:COH602 4.5 64.7 1.0 NE2 A:HIS207 4.6 31.0 1.0 CE1 A:HIS207 4.7 31.2 1.0 CD A:GLN203 4.9 27.0 1.0 HD1 A:HIS388 5.0 54.8 1.0

Cobalt binding site 2 out of 2 in the The Structure of Mefenamic 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 Mefenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co603 b:48.8 occ:1.00 CO B:COH603 0.0 48.8 1.0 NC B:COH603 2.0 74.0 1.0 NA B:COH603 2.0 67.3 1.0 NB B:COH603 2.1 65.8 1.0 ND B:COH603 2.1 70.2 1.0 NE2 B:HIS388 2.1 51.2 1.0 CD2 B:HIS388 3.0 52.0 1.0 C4C B:COH603 3.0 73.3 1.0 C4A B:COH603 3.0 65.3 1.0 C1C B:COH603 3.1 73.2 1.0 C1B B:COH603 3.1 63.3 1.0 C1A B:COH603 3.1 70.1 1.0 C1D B:COH603 3.1 69.5 1.0 C4D B:COH603 3.1 70.4 1.0 C4B B:COH603 3.1 67.3 1.0 CE1 B:HIS388 3.1 51.4 1.0 HD2 B:HIS388 3.2 70.0 1.0 HE1 B:HIS388 3.4 71.5 1.0 CHB B:COH603 3.4 63.3 1.0 CHD B:COH603 3.4 72.2 1.0 CHC B:COH603 3.4 70.6 1.0 CHA B:COH603 3.5 71.9 1.0 HE21 B:GLN203 3.8 61.5 1.0 HE1 B:HIS207 4.2 58.0 1.0 CG B:HIS388 4.2 52.9 1.0 ND1 B:HIS388 4.2 51.9 1.0 HG11 B:VAL447 4.2 68.4 1.0 C3C B:COH603 4.3 72.9 1.0 C2C B:COH603 4.3 73.4 1.0 C3A B:COH603 4.3 65.9 1.0 HE2 B:HIS207 4.3 58.4 1.0 NE2 B:GLN203 4.3 45.1 1.0 C2B B:COH603 4.3 62.2 1.0 C2A B:COH603 4.3 68.9 1.0 HG3 B:GLN203 4.3 49.3 1.0 C3B B:COH603 4.3 64.8 1.0 C2D B:COH603 4.3 65.9 1.0 HHD B:COH603 4.3 87.1 1.0 HHB B:COH603 4.3 76.5 1.0 C3D B:COH603 4.3 68.1 1.0 HHC B:COH603 4.4 85.2 1.0 HHA B:COH603 4.4 86.8 1.0 HE22 B:GLN203 4.6 61.5 1.0 CE1 B:HIS207 4.8 41.0 1.0 NE2 B:HIS207 4.8 41.9 1.0 HD1 B:HIS388 5.0 71.0 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