Cobalt in PDB 5kir: The Structure of Vioxx Bound to Human Cox-2

All present enzymatic activity of The Structure of Vioxx Bound to Human Cox-2:
1.14.99.1;

The structure of The Structure of Vioxx Bound to Human Cox-2, PDB code: 5kir 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)	30.03 / 2.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	126.989, 149.422, 185.055, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 22

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

Cobalt binding site 1 out of 2 in the The Structure of Vioxx Bound to Human Cox-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 Vioxx Bound to Human Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co602 b:97.5 occ:1.00 CO A:COH602 0.0 97.5 1.0 ND A:COH602 2.0 79.3 1.0 NA A:COH602 2.0 80.9 1.0 NC A:COH602 2.0 77.6 1.0 NB A:COH602 2.0 78.8 1.0 NE2 A:HIS388 2.2 77.3 1.0 C1C A:COH602 3.1 78.1 1.0 C1A A:COH602 3.1 80.0 1.0 C1D A:COH602 3.1 78.7 1.0 C4D A:COH602 3.1 78.2 1.0 C4A A:COH602 3.1 78.8 1.0 C1B A:COH602 3.1 77.8 1.0 C4B A:COH602 3.1 78.2 1.0 CD2 A:HIS388 3.1 79.0 1.0 C4C A:COH602 3.1 77.4 1.0 CE1 A:HIS388 3.2 78.5 1.0 HD2 A:HIS388 3.3 94.8 1.0 HE1 A:HIS388 3.4 94.2 1.0 CHC A:COH602 3.5 77.9 1.0 CHA A:COH602 3.6 78.3 1.0 CHD A:COH602 3.6 78.4 1.0 CHB A:COH602 3.6 78.5 1.0 HE21 A:GLN203 3.6 51.3 1.0 HE1 A:HIS207 3.9 63.8 1.0 HG3 A:GLN203 4.0 46.6 1.0 NE2 A:GLN203 4.2 42.7 1.0 ND1 A:HIS388 4.3 76.4 1.0 CG A:HIS388 4.3 77.8 1.0 C3A A:COH602 4.4 78.4 1.0 C3D A:COH602 4.4 78.2 1.0 C2A A:COH602 4.4 79.1 1.0 C2D A:COH602 4.4 77.4 1.0 C3B A:COH602 4.4 77.7 1.0 C2C A:COH602 4.4 76.7 1.0 HG11 A:VAL447 4.4 58.1 1.0 C2B A:COH602 4.4 77.0 1.0 C3C A:COH602 4.4 75.4 1.0 NE2 A:HIS207 4.5 49.8 1.0 CE1 A:HIS207 4.5 53.2 1.0 HE22 A:GLN203 4.5 51.3 1.0 HHC A:COH602 4.6 93.5 1.0 HHA A:COH602 4.6 94.0 1.0 HHD A:COH602 4.6 94.0 1.0 HHB A:COH602 4.7 94.2 1.0 CG A:GLN203 4.8 38.8 1.0 CD A:GLN203 4.9 43.2 1.0 HD11 A:LEU391 5.0 55.1 1.0

Cobalt binding site 2 out of 2 in the The Structure of Vioxx Bound to Human Cox-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 Vioxx Bound to Human Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co602 b:0.8 occ:1.00 CO B:COH602 0.0 0.8 1.0 ND B:COH602 2.0 98.2 1.0 NA B:COH602 2.0 96.8 1.0 NB B:COH602 2.0 96.4 1.0 NC B:COH602 2.0 0.3 1.0 NE2 B:HIS388 2.2 78.8 1.0 C1C B:COH602 3.1 0.7 1.0 C1D B:COH602 3.1 98.9 1.0 C1B B:COH602 3.1 96.8 1.0 C4D B:COH602 3.1 97.1 1.0 C1A B:COH602 3.1 96.0 1.0 C4A B:COH602 3.1 96.1 1.0 C4B B:COH602 3.1 98.0 1.0 CE1 B:HIS388 3.1 77.8 1.0 C4C B:COH602 3.1 0.9 1.0 CD2 B:HIS388 3.2 78.3 1.0 HE1 B:HIS388 3.3 93.3 1.0 HD2 B:HIS388 3.3 93.9 1.0 CHC B:COH602 3.5 99.8 1.0 CHD B:COH602 3.6 0.1 1.0 CHA B:COH602 3.6 96.5 1.0 CHB B:COH602 3.6 97.4 1.0 HE2 B:HIS207 3.9 72.2 1.0 HE21 B:GLN203 3.9 54.5 1.0 ND1 B:HIS388 4.3 76.3 1.0 CG B:HIS388 4.3 76.2 1.0 HG3 B:GLN203 4.3 46.1 1.0 HG11 B:VAL447 4.3 64.9 1.0 C3D B:COH602 4.4 97.1 1.0 C2D B:COH602 4.4 98.2 1.0 C3B B:COH602 4.4 97.1 1.0 C3A B:COH602 4.4 94.2 1.0 C2C B:COH602 4.4 0.5 1.0 C2B B:COH602 4.4 96.5 1.0 C3C B:COH602 4.4 0.3 1.0 C2A B:COH602 4.4 94.5 1.0 NE2 B:GLN203 4.4 45.4 1.0 NE2 B:HIS207 4.6 60.1 1.0 HE1 B:HIS207 4.6 72.2 1.0 HHC B:COH602 4.6 0.8 1.0 HHD B:COH602 4.6 0.1 1.0 HHA B:COH602 4.6 0.8 1.0 HHB B:COH602 4.6 0.9 1.0 HE22 B:GLN203 4.7 54.5 1.0 CE1 B:HIS207 4.9 60.1 1.0

B.J.Orlando, M.G.Malkowski. Crystal Structure of Rofecoxib Bound to Human Cyclooxygenase-2. Acta Crystallogr.,Sect.F V. 72 772 2016.
ISSN: ESSN 2053-230X
PubMed: 27710942
DOI: 10.1107/S2053230X16014230