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Atomistry » Copper » PDB 6vow-6xx3 » 6xtq » |
Copper in PDB 6xtq: Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B ComplexEnzymatic activity of Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex
All present enzymatic activity of Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex:
1.8.3.7; Protein crystallography data
The structure of Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex, PDB code: 6xtq
was solved by
F.Leisinger,
F.P.Seebeck,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6xtq:
The structure of Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex
(pdb code 6xtq). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex, PDB code: 6xtq: Copper binding site 1 out of 1 in 6xtqGo back to
Copper binding site 1 out
of 1 in the Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme - Fge:Cu:S:O2-1B Complex
![]() Mono view ![]() Stereo pair view
Reference:
F.Leisinger,
D.A.Miarzlou,
F.P.Seebeck.
Crystal Structure Reveals Non-Coordinative Binding of O2 to the Copper Center of the Formylglycine-Generating Enzyme To Be Published.
Page generated: Mon Jul 14 07:30:49 2025
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