Cobalt in PDB 3olu: X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of R513H Murine Cox-2

All present enzymatic activity of X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of R513H Murine Cox-2:
1.14.99.1;

The structure of X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of R513H Murine Cox-2, PDB code: 3olu 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)	19.99 / 2.35
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.312, 131.754, 180.022, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 21.4

The binding sites of Cobalt atom in the X-Ray Crystal Structure of 1-Arachidonoyl Glycerol Bound to the Cyclooxygenase Channel of R513H Murine Cox-2 (pdb code 3olu). 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 R513H Murine Cox-2, PDB code: 3olu:
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 R513H Murine Cox-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 R513H Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co620 b:29.0 occ:1.00 CO A:COH620 0.0 29.0 1.0 ND A:COH620 2.0 28.3 1.0 NC A:COH620 2.0 28.0 1.0 NA A:COH620 2.1 30.3 1.0 NB A:COH620 2.2 28.5 1.0 NE2 A:HIS388 2.5 24.9 1.0 C4D A:COH620 3.0 28.8 1.0 C1A A:COH620 3.0 32.7 1.0 C1D A:COH620 3.0 28.2 1.0 C4C A:COH620 3.0 28.3 1.0 C1C A:COH620 3.1 27.8 1.0 C4A A:COH620 3.1 31.4 1.0 C4B A:COH620 3.2 29.5 1.0 CD2 A:HIS388 3.2 24.8 1.0 O A:HOH724 3.2 37.4 1.0 C1B A:COH620 3.2 28.9 1.0 CHA A:COH620 3.3 32.4 1.0 CHD A:COH620 3.4 28.6 1.0 CHC A:COH620 3.5 28.6 1.0 CHB A:COH620 3.6 29.4 1.0 CE1 A:HIS388 3.6 25.8 1.0 C3D A:COH620 4.3 28.0 1.0 C2A A:COH620 4.3 35.2 1.0 C2D A:COH620 4.3 28.2 1.0 C3C A:COH620 4.3 27.9 1.0 C2C A:COH620 4.3 28.2 1.0 C3A A:COH620 4.3 33.8 1.0 NE2 A:GLN203 4.3 21.2 1.0 C3B A:COH620 4.4 29.9 1.0 CG A:HIS388 4.4 22.8 1.0 C2B A:COH620 4.5 28.9 1.0 NE2 A:HIS207 4.5 27.1 1.0 CE1 A:HIS207 4.6 24.7 1.0 ND1 A:HIS388 4.6 24.0 1.0 CG A:GLN203 4.9 16.4 1.0 CD A:GLN203 5.0 18.3 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 R513H Murine Cox-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 R513H Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co619 b:31.9 occ:1.00 CO B:COH619 0.0 31.9 1.0 NA B:COH619 2.0 35.0 1.0 ND B:COH619 2.1 33.6 1.0 NB B:COH619 2.1 33.8 1.0 NC B:COH619 2.1 33.4 1.0 NE2 B:HIS388 2.2 15.8 0.5 C4D B:COH619 3.0 34.1 1.0 C1D B:COH619 3.0 32.6 1.0 C1A B:COH619 3.1 35.9 1.0 C4A B:COH619 3.1 35.5 1.0 CE1 B:HIS388 3.1 16.3 0.5 C1B B:COH619 3.1 34.4 1.0 CD2 B:HIS388 3.1 17.3 0.5 C4C B:COH619 3.1 32.0 1.0 C1C B:COH619 3.2 33.5 1.0 C4B B:COH619 3.2 34.7 1.0 CHA B:COH619 3.4 35.0 1.0 CHD B:COH619 3.4 32.7 1.0 CHB B:COH619 3.4 34.8 1.0 CHC B:COH619 3.5 34.8 1.0 ND1 B:HIS388 4.2 17.4 0.5 CG B:HIS388 4.2 18.9 0.5 C2D B:COH619 4.3 33.4 1.0 C3D B:COH619 4.3 34.0 1.0 C2A B:COH619 4.3 39.0 1.0 C3A B:COH619 4.3 37.1 1.0 CD2 B:HIS388 4.3 22.1 0.5 C3C B:COH619 4.3 31.3 1.0 C2B B:COH619 4.3 35.9 1.0 C2C B:COH619 4.4 32.5 1.0 C3B B:COH619 4.4 36.6 1.0 NE2 B:GLN203 4.4 18.4 1.0 NE2 B:HIS207 4.6 22.7 1.0 CE1 B:HIS207 4.6 23.3 1.0 O B:HOH727 4.8 42.2 1.0 NE2 B:HIS388 4.8 23.6 0.5 CD B:GLN203 4.9 19.3 1.0 CG B:GLN203 4.9 17.9 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