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Atomistry » Calcium » PDB 5nn9-5oc9 » 5o2z | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5nn9-5oc9 » 5o2z » |
Calcium in PDB 5o2z: Domain Swap Dimer of the G167R Variant of Gelsolin Second DomainProtein crystallography data
The structure of Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain, PDB code: 5o2z
was solved by
F.Boni,
M.Milani,
E.Mastrangelo,
M.De Rosa,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5o2z:
The structure of Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain
(pdb code 5o2z). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain, PDB code: 5o2z: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 5o2zGo back to Calcium Binding Sites List in 5o2z
Calcium binding site 1 out
of 2 in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 5o2zGo back to Calcium Binding Sites List in 5o2z
Calcium binding site 2 out
of 2 in the Domain Swap Dimer of the G167R Variant of Gelsolin Second Domain
Mono view Stereo pair view
Reference:
F.Boni,
M.Milani,
A.Barbiroli,
L.Diomede,
E.Mastrangelo,
M.De Rosa.
Gelsolin Pathogenic GLY167ARG Mutation Promotes Domain-Swap Dimerization of the Protein. Hum. Mol. Genet. V. 27 53 2018.
Page generated: Mon Jul 15 09:41:32 2024
ISSN: ESSN 1460-2083 PubMed: 29069428 DOI: 10.1093/HMG/DDX383 |
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