Cobalt in PDB 3tzi: X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of G533V Murine Cox-2

All present enzymatic activity of X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of G533V Murine Cox-2:
1.14.99.1;

The structure of X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of G533V Murine Cox-2, PDB code: 3tzi 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 / 2.15
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	122.265, 133.508, 181.093, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of G533V Murine Cox-2 (pdb code 3tzi). 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 in the Cyclooxygenase Channel of G533V Murine Cox-2, PDB code: 3tzi:
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 in the Cyclooxygenase Channel of G533V 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 in the Cyclooxygenase Channel of G533V Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co619 b:38.9 occ:1.00 CO A:COH619 0.0 38.9 1.0 NC A:COH619 2.1 38.9 1.0 ND A:COH619 2.1 39.1 1.0 NA A:COH619 2.1 40.5 1.0 NB A:COH619 2.2 39.5 1.0 NE2 A:HIS388 2.5 33.0 1.0 C4C A:COH619 3.0 38.3 1.0 C1D A:COH619 3.1 38.3 1.0 C1C A:COH619 3.1 38.7 1.0 C4D A:COH619 3.1 38.9 1.0 C1A A:COH619 3.1 41.8 1.0 C4A A:COH619 3.1 41.5 1.0 O A:HOH934 3.1 43.5 1.0 C1B A:COH619 3.2 40.7 1.0 C4B A:COH619 3.2 40.1 1.0 CD2 A:HIS388 3.3 31.6 1.0 CHD A:COH619 3.4 37.6 1.0 CHA A:COH619 3.4 40.1 1.0 CHC A:COH619 3.5 39.9 1.0 CHB A:COH619 3.5 41.0 1.0 CE1 A:HIS388 3.6 33.3 1.0 NE2 A:GLN203 4.2 28.9 1.0 C3C A:COH619 4.3 38.1 1.0 C2C A:COH619 4.3 38.9 1.0 C2D A:COH619 4.3 38.1 1.0 C3D A:COH619 4.3 38.6 1.0 C2A A:COH619 4.3 43.9 1.0 C3A A:COH619 4.4 43.0 1.0 C2B A:COH619 4.4 40.8 1.0 C3B A:COH619 4.4 40.0 1.0 CE1 A:HIS207 4.5 31.9 1.0 CG A:HIS388 4.5 29.7 1.0 NE2 A:HIS207 4.5 33.2 1.0 ND1 A:HIS388 4.6 31.9 1.0 CD A:GLN203 4.9 26.9 1.0 CG A:GLN203 4.9 24.7 1.0

Cobalt binding site 2 out of 2 in the X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of G533V 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 in the Cyclooxygenase Channel of G533V Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co619 b:37.4 occ:1.00 CO B:COH619 0.0 37.4 1.0 NC B:COH619 2.1 37.5 1.0 ND B:COH619 2.1 38.4 1.0 NA B:COH619 2.1 39.3 1.0 NB B:COH619 2.1 38.1 1.0 NE2 B:HIS388 2.4 35.1 1.0 C1C B:COH619 3.1 37.4 1.0 C4D B:COH619 3.1 38.5 1.0 C4C B:COH619 3.1 37.0 1.0 C1D B:COH619 3.1 37.8 1.0 C4B B:COH619 3.1 37.7 1.0 C1A B:COH619 3.1 40.4 1.0 C1B B:COH619 3.1 37.8 1.0 C4A B:COH619 3.1 39.8 1.0 CD2 B:HIS388 3.2 33.4 1.0 O B:HOH841 3.3 38.9 1.0 CHA B:COH619 3.4 39.4 1.0 CHD B:COH619 3.4 36.9 1.0 CHC B:COH619 3.4 37.5 1.0 CE1 B:HIS388 3.5 34.5 1.0 CHB B:COH619 3.5 38.6 1.0 C2C B:COH619 4.3 37.1 1.0 NE2 B:GLN203 4.3 27.1 1.0 C3D B:COH619 4.3 39.0 1.0 C3C B:COH619 4.3 37.0 1.0 C2D B:COH619 4.3 37.9 1.0 C3B B:COH619 4.3 37.9 1.0 C2B B:COH619 4.3 38.0 1.0 C2A B:COH619 4.3 41.8 1.0 NE2 B:HIS207 4.3 31.8 1.0 C3A B:COH619 4.4 40.5 1.0 CG B:HIS388 4.4 31.9 1.0 ND1 B:HIS388 4.5 32.1 1.0 CE1 B:HIS207 4.6 31.4 1.0 CD B:GLN203 4.9 27.4 1.0 CG B:GLN203 5.0 25.8 1.0

A.J.Vecchio, B.J.Orlando, R.Nandagiri, M.G.Malkowski. Investigating Substrate Promiscuity in Cyclooxygenase-2: the Role of Arg-120 and Residues Lining the Hydrophobic Groove. J.Biol.Chem. V. 287 24619 2012.
ISSN: ISSN 0021-9258
PubMed: 22637474
DOI: 10.1074/JBC.M112.372243