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Atomistry » Calcium » PDB 5odc-5oyj » 5owo | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5odc-5oyj » 5owo » |
Calcium in PDB 5owo: Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom ResolutionProtein crystallography data
The structure of Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution, PDB code: 5owo
was solved by
L.Urnavicius,
C.K.Lau,
M.M.Elshenawy,
E.Morales-Rios,
C.Motz,
A.Yildiz,
A.P.Carter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5owo:
The structure of Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution
(pdb code 5owo). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution, PDB code: 5owo: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 5owoGo back to Calcium Binding Sites List in 5owo
Calcium binding site 1 out
of 2 in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 5owoGo back to Calcium Binding Sites List in 5owo
Calcium binding site 2 out
of 2 in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution
Mono view Stereo pair view
Reference:
L.Urnavicius,
C.K.Lau,
M.M.Elshenawy,
E.Morales-Rios,
C.Motz,
A.Yildiz,
A.P.Carter.
Cryo-Em Shows How Dynactin Recruits Two Dyneins For Faster Movement. Nature V. 554 202 2018.
Page generated: Mon Jul 15 09:54:48 2024
ISSN: ESSN 1476-4687 PubMed: 29420470 DOI: 10.1038/NATURE25462 |
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