Cobalt in PDB 3krk: X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of L531F Murine Cox-2

All present enzymatic activity of X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of L531F Murine Cox-2:
1.14.99.1;

The structure of X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of L531F Murine Cox-2, PDB code: 3krk was solved by A.J.Vecchio, D.M.Simmons, M.G.Malkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.92 / 2.40
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	120.790, 133.040, 180.654, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 22.8

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of L531F Murine Cox-2 (pdb code 3krk). 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 L531F Murine Cox-2, PDB code: 3krk:
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 L531F 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 L531F Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co625 b:86.2 occ:0.90 CO A:COH625 0.0 86.2 0.9 ND A:COH625 2.0 86.5 0.9 NB A:COH625 2.0 86.5 0.9 NC A:COH625 2.0 86.1 0.9 NA A:COH625 2.0 86.6 0.9 C4D A:COH625 3.0 86.6 0.9 C4C A:COH625 3.0 85.8 0.9 C1B A:COH625 3.0 86.6 0.9 C1C A:COH625 3.0 86.0 0.9 C4B A:COH625 3.0 86.5 0.9 C1D A:COH625 3.0 86.3 0.9 C1A A:COH625 3.1 86.9 0.9 C4A A:COH625 3.1 86.7 0.9 NE2 A:HIS388 3.2 30.5 0.5 CHC A:COH625 3.4 86.5 0.9 CHD A:COH625 3.5 86.1 0.9 CHA A:COH625 3.5 86.8 0.9 CHB A:COH625 3.5 86.7 0.9 CE1 A:HIS388 3.6 29.9 0.5 NE2 A:GLN203 4.0 25.9 1.0 NE2 A:HIS207 4.2 27.9 1.0 C3C A:COH625 4.2 85.3 0.9 CD2 A:HIS388 4.2 30.1 0.5 CE1 A:HIS207 4.3 28.3 1.0 C3B A:COH625 4.3 86.5 0.9 C2C A:COH625 4.3 85.5 0.9 C3D A:COH625 4.3 86.5 0.9 C2B A:COH625 4.3 86.5 0.9 C2D A:COH625 4.3 86.3 0.9 C2A A:COH625 4.4 86.9 0.9 C3A A:COH625 4.4 86.9 0.9 ND1 A:HIS388 4.7 29.5 0.5 CD A:GLN203 4.8 24.3 1.0 CD2 A:HIS388 4.9 28.0 0.5 O A:HOH897 4.9 38.3 1.0 CG A:GLN203 5.0 21.1 1.0

Cobalt binding site 2 out of 2 in the X-Ray Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Channel of L531F 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 L531F Murine Cox-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co626 b:79.4 occ:0.90 CO B:COH626 0.0 79.4 0.9 ND B:COH626 2.0 79.6 0.9 NB B:COH626 2.0 79.7 0.9 NC B:COH626 2.0 79.3 0.9 NA B:COH626 2.0 79.8 0.9 NE2 B:HIS388 2.9 33.1 0.5 C4D B:COH626 3.0 79.4 0.9 C4B B:COH626 3.0 79.4 0.9 C1B B:COH626 3.0 79.6 0.9 C1C B:COH626 3.0 79.0 0.9 C4C B:COH626 3.0 79.0 0.9 C1D B:COH626 3.1 79.3 0.9 C1A B:COH626 3.1 79.8 0.9 C4A B:COH626 3.1 79.9 0.9 CHC B:COH626 3.4 79.4 0.9 CHA B:COH626 3.5 79.5 0.9 CHB B:COH626 3.5 80.0 0.9 CHD B:COH626 3.5 79.1 0.9 CE1 B:HIS388 3.6 32.5 0.5 CD2 B:HIS388 3.9 33.1 0.5 C3B B:COH626 4.2 79.4 0.9 CE1 B:HIS207 4.2 32.2 1.0 C3C B:COH626 4.2 78.5 0.9 C3D B:COH626 4.3 79.5 0.9 C2B B:COH626 4.3 79.3 0.9 C2C B:COH626 4.3 78.6 0.9 C2D B:COH626 4.3 79.3 0.9 NE2 B:GLN203 4.3 29.0 1.0 NE2 B:HIS207 4.4 31.5 1.0 C3A B:COH626 4.4 79.9 0.9 C2A B:COH626 4.4 80.1 0.9 ND1 B:HIS388 4.7 32.4 0.5 CD2 B:HIS388 4.7 31.9 0.5 CG B:HIS388 4.9 32.4 0.5 CG B:GLN203 4.9 25.7 1.0 CD B:GLN203 4.9 27.9 1.0 NE2 B:HIS388 5.0 31.8 0.5

A.J.Vecchio, D.M.Simmons, M.G.Malkowski. Structural Basis of Fatty Acid Substrate Binding to Cyclooxygenase-2. J.Biol.Chem. V. 285 22152 2010.
ISSN: ISSN 0021-9258
PubMed: 20463020
DOI: 10.1074/JBC.M110.119867