Cobalt in PDB 5ikt: The Structure of Tolfenamic Acid Bound to Human Cyclooxygenase-2

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

The structure of The Structure of Tolfenamic Acid Bound to Human Cyclooxygenase-2, PDB code: 5ikt 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)	29.97 / 2.45
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	126.669, 149.759, 185.726, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22

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

Chlorine

(Cl)

2 atoms

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

Cobalt binding site 1 out of 2 in the The Structure of Tolfenamic 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 Tolfenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co602 b:51.3 occ:1.00 CO A:COH602 0.0 51.3 1.0 NC A:COH602 2.1 58.7 1.0 NB A:COH602 2.1 63.2 1.0 NA A:COH602 2.1 62.5 1.0 ND A:COH602 2.1 57.4 1.0 NE2 A:HIS388 2.1 68.8 1.0 C1C A:COH602 3.1 58.5 1.0 CD2 A:HIS388 3.1 56.8 1.0 C1D A:COH602 3.1 51.0 1.0 C4C A:COH602 3.1 54.5 1.0 C4B A:COH602 3.1 57.4 1.0 C4A A:COH602 3.1 60.7 1.0 C1B A:COH602 3.1 52.8 1.0 C1A A:COH602 3.1 55.0 1.0 C4D A:COH602 3.1 56.8 1.0 CE1 A:HIS388 3.2 62.9 1.0 HD2 A:HIS388 3.2 68.1 1.0 HE1 A:HIS388 3.4 75.4 1.0 CHD A:COH602 3.4 51.5 1.0 CHC A:COH602 3.4 52.4 1.0 CHB A:COH602 3.5 56.8 1.0 CHA A:COH602 3.5 61.4 1.0 HE21 A:GLN203 4.0 65.8 1.0 HG11 A:VAL447 4.0 97.6 1.0 HE1 A:HIS207 4.1 59.2 1.0 CG A:HIS388 4.2 54.3 1.0 ND1 A:HIS388 4.2 56.4 1.0 HE2 A:HIS207 4.3 84.0 1.0 C2C A:COH602 4.3 52.6 1.0 C3C A:COH602 4.3 53.8 1.0 C3A A:COH602 4.3 61.9 1.0 C2D A:COH602 4.3 51.1 1.0 C2A A:COH602 4.3 56.8 1.0 C3B A:COH602 4.3 52.3 1.0 C2B A:COH602 4.3 51.3 1.0 C3D A:COH602 4.3 57.2 1.0 NE2 A:GLN203 4.4 54.9 1.0 HHD A:COH602 4.4 61.8 1.0 HHB A:COH602 4.4 68.1 1.0 HHC A:COH602 4.4 62.8 1.0 HG3 A:GLN203 4.4 56.8 1.0 HHA A:COH602 4.4 73.7 1.0 HE22 A:GLN203 4.5 65.8 1.0 CE1 A:HIS207 4.7 49.4 1.0 NE2 A:HIS207 4.8 70.0 1.0 CG1 A:VAL447 4.9 81.4 1.0

Cobalt binding site 2 out of 2 in the The Structure of Tolfenamic 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 Tolfenamic Acid Bound to Human Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co602 b:45.3 occ:1.00 CO B:COH602 0.0 45.3 1.0 NC B:COH602 2.0 50.7 1.0 ND B:COH602 2.1 64.1 1.0 NB B:COH602 2.1 65.5 1.0 NA B:COH602 2.1 70.5 1.0 NE2 B:HIS388 2.1 62.9 1.0 C1C B:COH602 3.0 54.7 1.0 CD2 B:HIS388 3.0 64.3 1.0 C4B B:COH602 3.1 52.3 1.0 C4D B:COH602 3.1 53.6 1.0 C4C B:COH602 3.1 52.4 1.0 C1A B:COH602 3.1 57.2 1.0 C1D B:COH602 3.1 52.4 1.0 C4A B:COH602 3.1 65.5 1.0 C1B B:COH602 3.1 52.1 1.0 CE1 B:HIS388 3.2 74.5 1.0 HD2 B:HIS388 3.2 77.2 1.0 HE1 B:HIS388 3.4 89.4 1.0 CHC B:COH602 3.4 51.1 1.0 CHA B:COH602 3.4 53.8 1.0 CHD B:COH602 3.4 55.0 1.0 CHB B:COH602 3.5 55.0 1.0 HE21 B:GLN203 3.9 62.2 1.0 HE2 B:HIS207 4.1 63.8 1.0 HG11 B:VAL447 4.1 77.3 1.0 CG B:HIS388 4.2 67.9 1.0 ND1 B:HIS388 4.2 59.4 1.0 HE1 B:HIS207 4.2 54.0 1.0 C2C B:COH602 4.2 47.7 1.0 C3C B:COH602 4.3 47.4 1.0 HG3 B:GLN203 4.3 52.0 1.0 C3B B:COH602 4.3 52.1 1.0 C2A B:COH602 4.3 64.7 1.0 C3D B:COH602 4.3 56.6 1.0 C2D B:COH602 4.3 53.7 1.0 NE2 B:GLN203 4.3 51.9 1.0 C3A B:COH602 4.3 66.3 1.0 C2B B:COH602 4.4 49.5 1.0 HHC B:COH602 4.4 61.3 1.0 HHA B:COH602 4.4 64.5 1.0 HHD B:COH602 4.4 65.9 1.0 HHB B:COH602 4.4 66.0 1.0 HE22 B:GLN203 4.6 62.2 1.0 NE2 B:HIS207 4.7 53.1 1.0 CE1 B:HIS207 4.8 45.0 1.0 HD11 B:LEU391 4.9 63.8 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