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Atomistry » Magnesium » PDB 2xzv-2yaz » 2y08 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2xzv-2yaz » 2y08 » |
Magnesium in PDB 2y08: Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase TamlProtein crystallography data
The structure of Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase Taml, PDB code: 2y08
was solved by
J.C.Carlson,
S.Li,
S.S.Gunatilleke,
Y.Anzai,
D.A.Burr,
L.M.Podust,
D.H.Sherman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2y08:
The structure of Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase Taml also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase Taml
(pdb code 2y08). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase Taml, PDB code: 2y08: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2y08Go back to Magnesium Binding Sites List in 2y08
Magnesium binding site 1 out
of 2 in the Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase Taml
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 2y08Go back to Magnesium Binding Sites List in 2y08
Magnesium binding site 2 out
of 2 in the Structure of the Substrate-Free Fad-Dependent Tirandamycin Oxidase Taml
Mono view Stereo pair view
Reference:
J.C.Carlson,
S.Li,
S.S.Gunatilleke,
Y.Anzai,
D.A.Burr,
L.M.Podust,
D.H.Sherman.
Tirandamycin Biosynthesis Is Mediated By Co-Dependent Oxidative Enzymes Nat.Chem V. 3 628 2011.
Page generated: Wed Aug 14 07:22:13 2024
ISSN: ISSN 1755-4330 PubMed: 21778983 DOI: 10.1038/NCHEM.1087 |
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