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Atomistry » Sodium » PDB 2woi-2x2v » 2x2e | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 2woi-2x2v » 2x2e » |
Sodium in PDB 2x2e: Dynamin Gtpase Dimer, Long Axis FormEnzymatic activity of Dynamin Gtpase Dimer, Long Axis Form
All present enzymatic activity of Dynamin Gtpase Dimer, Long Axis Form:
3.6.5.5; Protein crystallography data
The structure of Dynamin Gtpase Dimer, Long Axis Form, PDB code: 2x2e
was solved by
J.S.Chappie,
S.Acharya,
M.Leonard,
S.L.Schmid,
F.Dyda,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2x2e:
The structure of Dynamin Gtpase Dimer, Long Axis Form also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Dynamin Gtpase Dimer, Long Axis Form
(pdb code 2x2e). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Dynamin Gtpase Dimer, Long Axis Form, PDB code: 2x2e: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 2x2eGo back to Sodium Binding Sites List in 2x2e
Sodium binding site 1 out
of 2 in the Dynamin Gtpase Dimer, Long Axis Form
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 2x2eGo back to Sodium Binding Sites List in 2x2e
Sodium binding site 2 out
of 2 in the Dynamin Gtpase Dimer, Long Axis Form
Mono view Stereo pair view
Reference:
J.S.Chappie,
S.Acharya,
M.Leonard,
S.L.Schmid,
F.Dyda.
G Domain Dimerization Controls Dynamin'S Assembly-Stimulated Gtpase Activity. Nature V. 465 435 2010.
Page generated: Tue Dec 15 05:58:46 2020
ISSN: ISSN 0028-0836 PubMed: 20428113 DOI: 10.1038/NATURE09032 |
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