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Atomistry » Calcium » PDB 1vfo-1w7c » 1vzh » |
Calcium in PDB 1vzh: Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced PhotoreductionEnzymatic activity of Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction
All present enzymatic activity of Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction:
1.15.1.2; Protein crystallography data
The structure of Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction, PDB code: 1vzh
was solved by
V.Adam,
A.Royant,
V.Niviere,
F.P.Molina-Heredia,
D.Bourgeois,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1vzh:
The structure of Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction
(pdb code 1vzh). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction, PDB code: 1vzh: Calcium binding site 1 out of 1 in 1vzhGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray Induced Photoreduction
![]() Mono view ![]() Stereo pair view
Reference:
V.Adam,
A.Royant,
V.Niviere,
F.P.Molina-Heredia,
D.Bourgeois.
Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion Upon X-Ray-Induced Photo-Reduction. Structure V. 12 1729 2004.
Page generated: Fri Jul 12 06:56:54 2024
ISSN: ISSN 0969-2126 PubMed: 15341736 DOI: 10.1016/J.STR.2004.07.013 |
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