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Atomistry » Aluminium » PDB 1vfx-2x2f » 2x2e | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Aluminium » PDB 1vfx-2x2f » 2x2e » |
Aluminium 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:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Dynamin Gtpase Dimer, Long Axis Form
(pdb code 2x2e). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Dynamin Gtpase Dimer, Long Axis Form, PDB code: 2x2e: Jump to Aluminium binding site number: 1; 2; Aluminium binding site 1 out of 2 in 2x2eGo back to![]() ![]()
Aluminium binding site 1 out
of 2 in the Dynamin Gtpase Dimer, Long Axis Form
![]() Mono view ![]() Stereo pair view
Aluminium binding site 2 out of 2 in 2x2eGo back to![]() ![]()
Aluminium 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: Sun Jul 6 21:43:33 2025
ISSN: ISSN 0028-0836 PubMed: 20428113 DOI: 10.1038/NATURE09032 |
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