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Atomistry » Zinc » PDB 2hpy-2i7v » 2hu9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2hpy-2i7v » 2hu9 » |
Zinc in PDB 2hu9: X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal DomainProtein crystallography data
The structure of X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal Domain, PDB code: 2hu9
was solved by
M.H.Sazinsky,
B.Lemoine,
J.M.Arguello,
A.C.Rosenzweig,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2hu9:
The structure of X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal Domain also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal Domain
(pdb code 2hu9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal Domain, PDB code: 2hu9: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2hu9Go back to![]() ![]()
Zinc binding site 1 out
of 2 in the X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal Domain
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 2hu9Go back to![]() ![]()
Zinc binding site 2 out
of 2 in the X-Ray Structure of the Archaeoglobus Fulgidus Copz N- Terminal Domain
![]() Mono view ![]() Stereo pair view
Reference:
M.H.Sazinsky,
B.Lemoine,
M.Orofino,
R.Davydov,
K.Z.Bencze,
T.L.Stemmler,
B.M.Hoffman,
J.M.Arguello,
A.C.Rosenzweig.
Characterization and Structure of A ZN2+ and [2FE-2S]-Containing Copper Chaperone From Archaeoglobus Fulgidus. J.Biol.Chem. V. 282 25950 2007.
Page generated: Wed Dec 16 03:30:24 2020
ISSN: ISSN 0021-9258 PubMed: 17609202 DOI: 10.1074/JBC.M703311200 |
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