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Atomistry » Calcium » PDB 1de4-1dv8 » 1dsy | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1de4-1dv8 » 1dsy » |
Calcium in PDB 1dsy: C2 Domain From Protein Kinase C (Alpha) Complexed with CA2+ and PhosphatidylserineProtein crystallography data
The structure of C2 Domain From Protein Kinase C (Alpha) Complexed with CA2+ and Phosphatidylserine, PDB code: 1dsy
was solved by
N.Verdaguer,
S.Corbalan-Garcia,
W.F.Ochoa,
I.Fita,
J.C.Gomez-Fernandez,
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 C2 Domain From Protein Kinase C (Alpha) Complexed with CA2+ and Phosphatidylserine
(pdb code 1dsy). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the C2 Domain From Protein Kinase C (Alpha) Complexed with CA2+ and Phosphatidylserine, PDB code: 1dsy: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1dsyGo back to Calcium Binding Sites List in 1dsy
Calcium binding site 1 out
of 2 in the C2 Domain From Protein Kinase C (Alpha) Complexed with CA2+ and Phosphatidylserine
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1dsyGo back to Calcium Binding Sites List in 1dsy
Calcium binding site 2 out
of 2 in the C2 Domain From Protein Kinase C (Alpha) Complexed with CA2+ and Phosphatidylserine
Mono view Stereo pair view
Reference:
N.Verdaguer,
S.Corbalan-Garcia,
W.F.Ochoa,
I.Fita,
J.C.Gomez-Fernandez.
Ca(2+) Bridges the C2 Membrane-Binding Domain of Protein Kinase Calpha Directly to Phosphatidylserine. Embo J. V. 18 6329 1999.
Page generated: Thu Jul 11 07:38:22 2024
ISSN: ISSN 0261-4189 PubMed: 10562545 DOI: 10.1093/EMBOJ/18.22.6329 |
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