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Atomistry » Calcium » PDB 2yi1-2z8s » 2yv9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 2yi1-2z8s » 2yv9 » |
Calcium in PDB 2yv9: Crystal Structure of the Clic Homologue Exc-4 From C. ElegansProtein crystallography data
The structure of Crystal Structure of the Clic Homologue Exc-4 From C. Elegans, PDB code: 2yv9
was solved by
S.J.Harrop,
D.R.Littler,
P.M.G.Curmi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of the Clic Homologue Exc-4 From C. Elegans
(pdb code 2yv9). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Clic Homologue Exc-4 From C. Elegans, PDB code: 2yv9: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 2yv9Go back to Calcium Binding Sites List in 2yv9
Calcium binding site 1 out
of 2 in the Crystal Structure of the Clic Homologue Exc-4 From C. Elegans
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 2yv9Go back to Calcium Binding Sites List in 2yv9
Calcium binding site 2 out
of 2 in the Crystal Structure of the Clic Homologue Exc-4 From C. Elegans
Mono view Stereo pair view
Reference:
D.R.Littler,
S.J.Harrop,
L.J.Brown,
G.J.Pankhurst,
A.V.Mynott,
P.Luciani,
R.A.Mandyam,
M.Mazzanti,
S.Tanda,
M.A.Berryman,
S.N.Breit,
P.M.G.Curmi.
Comparison of Vertebrate and Invertebrate Clic Proteins: the Crystal Structures of Caenorhabditis Elegans Exc-4 and Drosophila Melanogaster Dmclic Proteins V. 71 364 2007.
Page generated: Fri Jul 12 19:35:59 2024
ISSN: ISSN 0887-3585 PubMed: 17985355 DOI: 10.1002/PROT.21704 |
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