Cobalt in PDB 3olt: X-Ray Crystal Structure of Arachidonic Acid Bound to the Cyclooxygenase Channel of R513H Murine Cox-2

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

The structure of X-Ray Crystal Structure of Arachidonic Acid Bound to the Cyclooxygenase Channel of R513H Murine Cox-2, PDB code: 3olt 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)	19.86 / 2.45
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.148, 132.048, 180.758, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 21.9

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Arachidonic Acid Bound to the Cyclooxygenase Channel of R513H Murine Cox-2 (pdb code 3olt). 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 Arachidonic Acid Bound to the Cyclooxygenase Channel of R513H Murine Cox-2, PDB code: 3olt:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the X-Ray Crystal Structure of Arachidonic Acid 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 Arachidonic Acid Bound to the Cyclooxygenase Channel of R513H Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co621 b:40.3 occ:1.00 CO A:COH621 0.0 40.3 1.0 ND A:COH621 2.0 40.7 1.0 NC A:COH621 2.1 40.0 1.0 NA A:COH621 2.1 42.7 1.0 NB A:COH621 2.2 40.5 1.0 NE2 A:HIS388 2.3 19.7 0.5 C4D A:COH621 3.0 41.8 1.0 C1D A:COH621 3.0 41.0 1.0 C1A A:COH621 3.0 44.6 1.0 C4C A:COH621 3.1 40.2 1.0 C1C A:COH621 3.1 40.0 1.0 C4B A:COH621 3.2 40.6 1.0 C4A A:COH621 3.2 43.3 1.0 CD2 A:HIS388 3.2 20.6 0.5 CE1 A:HIS388 3.2 19.2 0.5 C1B A:COH621 3.3 40.8 1.0 O A:HOH782 3.3 36.7 1.0 CHA A:COH621 3.3 43.5 1.0 CHD A:COH621 3.4 40.9 1.0 CHC A:COH621 3.5 39.8 1.0 CHB A:COH621 3.6 41.7 1.0 NE2 A:GLN203 4.2 30.8 1.0 C3D A:COH621 4.2 41.2 1.0 C2D A:COH621 4.2 40.7 1.0 ND1 A:HIS388 4.3 20.9 0.5 C3C A:COH621 4.3 40.7 1.0 C2C A:COH621 4.3 40.7 1.0 C2A A:COH621 4.3 48.3 1.0 CG A:HIS388 4.3 21.8 0.5 C3A A:COH621 4.4 46.2 1.0 C3B A:COH621 4.4 40.9 1.0 C2B A:COH621 4.5 40.6 1.0 CE1 A:HIS207 4.6 32.8 1.0 CD2 A:HIS388 4.6 24.5 0.5 NE2 A:HIS207 4.6 34.8 1.0 CG A:GLN203 4.8 25.7 1.0 CD A:GLN203 4.9 29.6 1.0

Cobalt binding site 2 out of 2 in the X-Ray Crystal Structure of Arachidonic Acid 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 Arachidonic Acid Bound to the Cyclooxygenase Channel of R513H Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co619 b:40.5 occ:1.00 CO B:COH619 0.0 40.5 1.0 NB B:COH619 2.1 43.2 1.0 NA B:COH619 2.1 44.7 1.0 NC B:COH619 2.1 42.4 1.0 ND B:COH619 2.1 42.9 1.0 NE2 B:HIS388 2.7 39.8 1.0 C4D B:COH619 3.1 42.5 1.0 C1B B:COH619 3.1 44.1 1.0 C4B B:COH619 3.1 42.8 1.0 C1A B:COH619 3.1 45.4 1.0 C1C B:COH619 3.1 41.9 1.0 C1D B:COH619 3.1 41.7 1.0 C4A B:COH619 3.1 45.4 1.0 C4C B:COH619 3.1 41.4 1.0 CHA B:COH619 3.4 44.1 1.0 CD2 B:HIS388 3.4 37.8 1.0 CHC B:COH619 3.4 42.7 1.0 CHB B:COH619 3.4 45.1 1.0 CHD B:COH619 3.5 42.1 1.0 CE1 B:HIS388 3.9 39.0 1.0 NE2 B:GLN203 4.2 32.8 1.0 O B:HOH780 4.2 50.8 1.0 C3D B:COH619 4.3 42.6 1.0 C3B B:COH619 4.3 44.4 1.0 C2B B:COH619 4.3 45.1 1.0 C2D B:COH619 4.3 42.2 1.0 C2C B:COH619 4.3 41.5 1.0 C3C B:COH619 4.3 40.1 1.0 C2A B:COH619 4.4 48.9 1.0 C3A B:COH619 4.4 47.0 1.0 NE2 B:HIS207 4.7 35.9 1.0 CG B:HIS388 4.7 36.1 1.0 CE1 B:HIS207 4.8 33.6 1.0 CD B:GLN203 4.9 32.7 1.0 ND1 B:HIS388 4.9 38.2 1.0 CG B:GLN203 4.9 28.8 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