Cobalt in PDB 3mdl: X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2

All present enzymatic activity of X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2:
1.14.99.1;

The structure of X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2, PDB code: 3mdl was solved by A.J.Vecchio, M.G.Malkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.97 / 2.20
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	118.958, 131.773, 179.858, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 21.5

The binding sites of Cobalt atom in the X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 (pdb code 3mdl). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2, PDB code: 3mdl:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co614 b:48.4 occ:1.00 CO A:COH614 0.0 48.4 1.0 NC A:COH614 2.0 48.7 1.0 ND A:COH614 2.1 48.7 1.0 NA A:COH614 2.1 50.0 1.0 NB A:COH614 2.1 48.9 1.0 NE2 A:HIS388 2.3 18.6 0.5 C4C A:COH614 3.0 48.5 1.0 C1D A:COH614 3.0 48.6 1.0 C4D A:COH614 3.1 48.6 1.0 C1C A:COH614 3.1 48.5 1.0 CE1 A:HIS388 3.1 18.1 0.5 C1A A:COH614 3.1 50.8 1.0 C4B A:COH614 3.1 48.7 1.0 C4A A:COH614 3.2 50.4 1.0 C1B A:COH614 3.2 48.9 1.0 CD2 A:HIS388 3.3 18.6 0.5 CHD A:COH614 3.4 48.3 1.0 CHA A:COH614 3.4 50.0 1.0 CHC A:COH614 3.4 48.6 1.0 CHB A:COH614 3.5 49.5 1.0 NE2 A:GLN203 4.2 24.6 1.0 ND1 A:HIS388 4.2 18.2 0.5 O A:HOH1090 4.2 60.1 1.0 C3C A:COH614 4.3 48.4 1.0 C2C A:COH614 4.3 48.5 1.0 C3D A:COH614 4.3 48.1 1.0 C2D A:COH614 4.3 48.2 1.0 C2A A:COH614 4.4 52.3 1.0 CG A:HIS388 4.4 18.6 0.5 C3A A:COH614 4.4 51.5 1.0 C3B A:COH614 4.4 48.9 1.0 CD2 A:HIS388 4.4 19.0 0.5 C2B A:COH614 4.4 49.0 1.0 NE2 A:HIS207 4.5 27.7 1.0 CE1 A:HIS207 4.6 28.0 1.0 NE2 A:HIS388 4.8 20.0 0.5 CD A:GLN203 4.8 22.8 1.0 CG A:GLN203 4.9 20.1 1.0 CG1 A:VAL447 4.9 29.6 1.0

Cobalt binding site 2 out of 2 in the X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co615 b:44.6 occ:1.00 CO B:COH615 0.0 44.6 1.0 NC B:COH615 2.0 44.5 1.0 ND B:COH615 2.1 44.9 1.0 NB B:COH615 2.1 44.6 1.0 NA B:COH615 2.1 45.8 1.0 NE2 B:HIS388 2.3 24.1 0.5 C4C B:COH615 3.0 44.7 1.0 C1D B:COH615 3.0 44.8 1.0 C1C B:COH615 3.1 44.1 1.0 C4D B:COH615 3.1 44.7 1.0 C4B B:COH615 3.1 44.7 1.0 C1A B:COH615 3.1 46.9 1.0 C1B B:COH615 3.1 45.0 1.0 C4A B:COH615 3.2 46.3 1.0 CE1 B:HIS388 3.2 23.5 0.5 CD2 B:HIS388 3.2 24.6 0.5 CHD B:COH615 3.4 44.9 1.0 CHC B:COH615 3.4 44.3 1.0 CHA B:COH615 3.5 45.9 1.0 CHB B:COH615 3.5 45.7 1.0 C3C B:COH615 4.2 44.3 1.0 C2C B:COH615 4.3 44.2 1.0 C2D B:COH615 4.3 44.7 1.0 ND1 B:HIS388 4.3 24.0 0.5 C3D B:COH615 4.3 44.3 1.0 C3B B:COH615 4.3 44.4 1.0 CG B:HIS388 4.4 24.5 0.5 CD2 B:HIS388 4.4 24.9 0.5 C2B B:COH615 4.4 44.5 1.0 C2A B:COH615 4.4 48.7 1.0 C3A B:COH615 4.4 47.4 1.0 CE1 B:HIS207 4.4 21.5 1.0 NE2 B:GLN203 4.5 21.1 1.0 NE2 B:HIS207 4.5 22.2 1.0 NE2 B:HIS388 4.7 25.9 0.5 CG B:GLN203 4.9 16.0 1.0 CD B:GLN203 5.0 19.6 1.0

A.J.Vecchio, M.G.Malkowski. The Structural Basis of Endocannabinoid Oxygenation By Cyclooxygenase-2. J.Biol.Chem. V. 286 20736 2011.
ISSN: ISSN 0021-9258
PubMed: 21489986
DOI: 10.1074/JBC.M111.230367