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Atomistry » Calcium » PDB 1de4-1dv8 » 1deg » |
Calcium in PDB 1deg: The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal StructureProtein crystallography data
The structure of The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure, PDB code: 1deg
was solved by
S.Raghunathan,
R.Chandross,
B.P.Cheng,
A.Persechini,
S.E.Sobottk,
R.H.Kretsinger,
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 The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure
(pdb code 1deg). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure, PDB code: 1deg: Jump to Calcium binding site number: 1; 2; 3; 4; Calcium binding site 1 out of 4 in 1degGo back to Calcium Binding Sites List in 1deg
Calcium binding site 1 out
of 4 in the The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure
Mono view Stereo pair view
Calcium binding site 2 out of 4 in 1degGo back to Calcium Binding Sites List in 1deg
Calcium binding site 2 out
of 4 in the The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure
Mono view Stereo pair view
Calcium binding site 3 out of 4 in 1degGo back to Calcium Binding Sites List in 1deg
Calcium binding site 3 out
of 4 in the The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure
Mono view Stereo pair view
Calcium binding site 4 out of 4 in 1degGo back to Calcium Binding Sites List in 1deg
Calcium binding site 4 out
of 4 in the The Linker of Des-GLU84 Calmodulin Is Bent As Seen in the Crystal Structure
Mono view Stereo pair view
Reference:
S.Raghunathan,
R.J.Chandross,
B.P.Cheng,
A.Persechini,
S.E.Sobottka,
R.H.Kretsinger.
The Linker of Des-GLU84-Calmodulin Is Bent. Proc.Natl.Acad.Sci.Usa V. 90 6869 1993.
Page generated: Thu Jul 11 07:32:13 2024
ISSN: ISSN 0027-8424 PubMed: 8341712 DOI: 10.1073/PNAS.90.14.6869 |
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