Cobalt in PDB 4e1g: X-Ray Crystal Structure of Alpha-Linolenic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2

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

The structure of X-Ray Crystal Structure of Alpha-Linolenic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2, PDB code: 4e1g 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)	20.00 / 2.10
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	120.378, 132.131, 180.438, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 20.3

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Alpha-Linolenic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 (pdb code 4e1g). 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 Alpha-Linolenic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2, PDB code: 4e1g:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the X-Ray Crystal Structure of Alpha-Linolenic 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 Alpha-Linolenic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co702 b:78.2 occ:1.00 CO A:COH702 0.0 78.2 1.0 NC A:COH702 2.1 76.7 1.0 ND A:COH702 2.2 77.4 1.0 NA A:COH702 2.2 79.6 1.0 NB A:COH702 2.3 78.3 1.0 NE2 A:HIS388 2.7 33.9 0.5 C1C A:COH702 3.1 76.4 1.0 C4D A:COH702 3.1 77.8 1.0 C4B A:COH702 3.1 78.4 1.0 C1A A:COH702 3.2 81.1 1.0 C4C A:COH702 3.2 75.0 1.0 C1D A:COH702 3.2 76.7 1.0 C4A A:COH702 3.3 80.2 1.0 C1B A:COH702 3.3 77.6 1.0 CHC A:COH702 3.4 78.3 1.0 CD2 A:HIS388 3.4 32.1 0.5 CHA A:COH702 3.4 79.8 1.0 O A:HOH1129 3.5 55.0 1.0 CHD A:COH702 3.5 76.4 1.0 CE1 A:HIS388 3.7 34.8 0.5 CHB A:COH702 3.7 78.8 1.0 NE2 A:GLN203 4.2 42.8 1.0 C3D A:COH702 4.3 76.0 1.0 C2C A:COH702 4.3 74.3 1.0 C3C A:COH702 4.4 72.2 1.0 C2D A:COH702 4.4 76.1 1.0 C2A A:COH702 4.4 82.7 1.0 C3B A:COH702 4.4 76.6 1.0 C3A A:COH702 4.4 81.8 1.0 CE1 A:HIS207 4.5 49.1 1.0 C2B A:COH702 4.5 76.8 1.0 NE2 A:HIS207 4.5 46.1 1.0 CG A:HIS388 4.5 29.2 0.5 ND1 A:HIS388 4.6 31.1 0.5 CD A:GLN203 4.9 35.5 1.0

Cobalt binding site 2 out of 2 in the X-Ray Crystal Structure of Alpha-Linolenic 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 Alpha-Linolenic Acid Bound to the Cyclooxygenase Channel of Cyclooxygenase-2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co702 b:75.8 occ:1.00 CO B:COH702 0.0 75.8 1.0 NC B:COH702 2.2 75.6 1.0 NB B:COH702 2.2 76.9 1.0 NA B:COH702 2.2 77.1 1.0 ND B:COH702 2.3 75.2 1.0 NE2 B:HIS388 2.4 38.8 0.5 C1C B:COH702 3.1 75.3 1.0 C4B B:COH702 3.1 76.6 1.0 C1B B:COH702 3.2 76.8 1.0 C4A B:COH702 3.2 77.6 1.0 C4D B:COH702 3.2 73.8 1.0 C4C B:COH702 3.2 73.5 1.0 C1A B:COH702 3.2 76.6 1.0 CD2 B:HIS388 3.2 36.1 0.5 C1D B:COH702 3.2 73.3 1.0 CHC B:COH702 3.4 77.0 1.0 CE1 B:HIS388 3.4 37.5 0.5 CHB B:COH702 3.5 77.5 1.0 CHA B:COH702 3.5 74.6 1.0 CHD B:COH702 3.5 73.7 1.0 C3D B:COH702 4.4 72.8 1.0 C3B B:COH702 4.4 75.5 1.0 C2C B:COH702 4.4 72.7 1.0 C2B B:COH702 4.4 76.7 1.0 C3C B:COH702 4.4 71.3 1.0 C2D B:COH702 4.4 72.0 1.0 C3A B:COH702 4.4 78.2 1.0 NE2 B:GLN203 4.4 36.5 1.0 C2A B:COH702 4.4 78.5 1.0 CG B:HIS388 4.4 33.3 0.5 ND1 B:HIS388 4.5 35.7 0.5 CE1 B:HIS207 4.6 46.8 1.0 NE2 B:HIS207 4.6 45.6 1.0 CD2 B:HIS388 4.7 28.1 0.5 NE2 B:HIS388 5.0 26.1 0.5

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