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Atomistry » Magnesium » PDB 4mfe-4mpj » 4mn0 » |
Magnesium in PDB 4mn0: Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the CA2+-Loaded Apoprotein Conformation StateProtein crystallography data
The structure of Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the CA2+-Loaded Apoprotein Conformation State, PDB code: 4mn0
was solved by
Z.J.Liu,
G.A.Stepanyuk,
E.S.Vysotski,
J.Lee,
J.P.Rose,
B.C.Wang,
Southeastcollaboratory For Structural Genomics (Secsg),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4mn0:
The structure of Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the CA2+-Loaded Apoprotein Conformation State also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the CA2+-Loaded Apoprotein Conformation State
(pdb code 4mn0). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the CA2+-Loaded Apoprotein Conformation State, PDB code: 4mn0: Magnesium binding site 1 out of 1 in 4mn0Go back to Magnesium Binding Sites List in 4mn0
Magnesium binding site 1 out
of 1 in the Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the CA2+-Loaded Apoprotein Conformation State
Mono view Stereo pair view
Reference:
G.A.Stepanyuk,
Z.J.Liu,
L.P.Burakova,
J.Lee,
J.Rose,
E.S.Vysotski,
B.C.Wang.
Spatial Structure of the Novel Light-Sensitive Photoprotein Berovin From the Ctenophore Beroe Abyssicola in the Ca(2+)-Loaded Apoprotein Conformation State. Biochim.Biophys.Acta V.1834 2139 2013.
Page generated: Mon Dec 14 19:13:01 2020
ISSN: ISSN 0006-3002 PubMed: 23891746 DOI: 10.1016/J.BBAPAP.2013.07.006 |
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