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Atomistry » Aluminium » PDB 1a6e-1tx4 » 1ihu | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Aluminium » PDB 1a6e-1tx4 » 1ihu » |
Aluminium in PDB 1ihu: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3Enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3
All present enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3:
3.6.3.16; Protein crystallography data
The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu
was solved by
T.Zhou,
S.Radaev,
B.P.Rosen,
D.L.Gatti,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1ihu:
The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3
(pdb code 1ihu). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu: Aluminium binding site 1 out of 1 in 1ihuGo back to Aluminium Binding Sites List in 1ihu
Aluminium binding site 1 out
of 1 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3
Mono view Stereo pair view
Reference:
T.Zhou,
S.Radaev,
B.P.Rosen,
D.L.Gatti.
Conformational Changes in Four Regions of the Escherichia Coli Arsa Atpase Link Atp Hydrolysis to Ion Translocation. J.Biol.Chem. V. 276 30414 2001.
Page generated: Sat Dec 12 01:30:14 2020
ISSN: ISSN 0021-9258 PubMed: 11395509 DOI: 10.1074/JBC.M103671200 |
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