Cobalt in PDB 3hs6: X-Ray Crystal Structure of Eicosapentaenoic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2

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

The structure of X-Ray Crystal Structure of Eicosapentaenoic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2, PDB code: 3hs6 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)	19.95 / 2.40
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.851, 132.336, 180.290, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 22.3

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Eicosapentaenoic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 (pdb code 3hs6). 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 Eicosapentaenoic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2, PDB code: 3hs6:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the X-Ray Crystal Structure of Eicosapentaenoic Acid 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 Eicosapentaenoic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co619 b:94.6 occ:1.00 CO A:COH619 0.0 94.6 1.0 NA A:COH619 2.1 94.9 1.0 NC A:COH619 2.1 94.5 1.0 NB A:COH619 2.1 94.6 1.0 ND A:COH619 2.1 94.6 1.0 NE2 A:HIS388 2.5 31.4 0.5 C4D A:COH619 3.1 94.3 1.0 C1A A:COH619 3.1 94.9 1.0 C1D A:COH619 3.1 94.3 1.0 C4C A:COH619 3.1 94.1 1.0 C1C A:COH619 3.1 94.4 1.0 C4B A:COH619 3.1 94.5 1.0 C4A A:COH619 3.1 94.8 1.0 C1B A:COH619 3.1 94.4 1.0 CE1 A:HIS388 3.3 31.1 0.5 CHA A:COH619 3.4 94.6 1.0 CHD A:COH619 3.5 94.3 1.0 CHC A:COH619 3.5 94.5 1.0 CD2 A:HIS388 3.5 31.7 0.5 CHB A:COH619 3.5 94.5 1.0 C3D A:COH619 4.3 93.8 1.0 C2D A:COH619 4.3 93.8 1.0 C2A A:COH619 4.3 95.3 1.0 C3C A:COH619 4.3 93.7 1.0 C2C A:COH619 4.3 94.0 1.0 C3A A:COH619 4.3 95.1 1.0 C3B A:COH619 4.4 94.1 1.0 C2B A:COH619 4.4 94.2 1.0 ND1 A:HIS388 4.4 31.6 0.5 NE2 A:HIS207 4.5 34.4 1.0 CG A:HIS388 4.5 31.3 0.5 NE2 A:GLN203 4.6 33.5 1.0 CE1 A:HIS207 4.6 35.6 1.0 CD2 A:HIS388 4.6 32.3 0.5 NE2 A:HIS388 5.0 32.5 0.5 CG1 A:VAL447 5.0 34.8 1.0

Cobalt binding site 2 out of 2 in the X-Ray Crystal Structure of Eicosapentaenoic Acid 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 Eicosapentaenoic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co619 b:85.7 occ:1.00 CO B:COH619 0.0 85.7 1.0 NA B:COH619 2.1 85.9 1.0 NB B:COH619 2.1 85.9 1.0 NC B:COH619 2.1 85.5 1.0 ND B:COH619 2.1 85.4 1.0 NE2 B:HIS388 2.5 34.3 0.5 C4D B:COH619 3.1 85.1 1.0 C1A B:COH619 3.1 86.2 1.0 C1D B:COH619 3.1 84.9 1.0 C4B B:COH619 3.1 85.9 1.0 C4A B:COH619 3.1 86.1 1.0 C1B B:COH619 3.1 85.8 1.0 C1C B:COH619 3.1 85.4 1.0 C4C B:COH619 3.1 85.1 1.0 CE1 B:HIS388 3.4 34.0 0.5 CHA B:COH619 3.4 85.6 1.0 CD2 B:HIS388 3.5 34.3 0.5 CHC B:COH619 3.5 85.8 1.0 CHB B:COH619 3.5 86.0 1.0 CHD B:COH619 3.5 85.1 1.0 O B:HOH750 3.5 44.0 1.0 C3D B:COH619 4.2 84.5 1.0 C2D B:COH619 4.3 84.5 1.0 C2A B:COH619 4.3 86.5 1.0 C3A B:COH619 4.3 86.2 1.0 C3B B:COH619 4.3 85.6 1.0 C2B B:COH619 4.3 85.7 1.0 C2C B:COH619 4.4 85.0 1.0 C3C B:COH619 4.4 84.7 1.0 ND1 B:HIS388 4.5 34.2 0.5 CD2 B:HIS388 4.5 34.5 0.5 NE2 B:GLN203 4.5 32.4 1.0 CG B:HIS388 4.6 34.4 0.5 CE1 B:HIS207 4.6 36.2 1.0 NE2 B:HIS207 4.7 35.6 1.0 NE2 B:HIS388 4.9 34.5 0.5 CG1 B:VAL447 4.9 33.2 1.0

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