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Atomistry » Cobalt » PDB 1hv9-1nr5 » 1igx | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 1hv9-1nr5 » 1igx » |
Cobalt in PDB 1igx: Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1.Enzymatic activity of Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1.
All present enzymatic activity of Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1.:
1.14.99.1; Protein crystallography data
The structure of Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1., PDB code: 1igx
was solved by
M.G.Malkowski,
E.D.Thuresson,
W.L.Smith,
R.M.Garavito,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1.
(pdb code 1igx). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1., PDB code: 1igx: Cobalt binding site 1 out of 1 in 1igxGo back to![]() ![]()
Cobalt binding site 1 out
of 1 in the Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1.
![]() Mono view ![]() Stereo pair view
Reference:
M.G.Malkowski,
E.D.Thuresson,
K.M.Lakkides,
C.J.Rieke,
R.Micielli,
W.L.Smith,
R.M.Garavito.
Structure of Eicosapentaenoic and Linoleic Acids in the Cyclooxygenase Site of Prostaglandin Endoperoxide H Synthase-1. J.Biol.Chem. V. 276 37547 2001.
Page generated: Tue Jul 30 14:22:44 2024
ISSN: ISSN 0021-9258 PubMed: 11477109 DOI: 10.1074/JBC.M105982200 |
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