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Atomistry » Calcium » PDB 3ecj-3eqd » 3ehj | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 3ecj-3eqd » 3ehj » |
Calcium in PDB 3ehj: Crystal Structure of Deskc-H188V in Complex with Amp-PcpEnzymatic activity of Crystal Structure of Deskc-H188V in Complex with Amp-Pcp
All present enzymatic activity of Crystal Structure of Deskc-H188V in Complex with Amp-Pcp:
2.7.13.3; Protein crystallography data
The structure of Crystal Structure of Deskc-H188V in Complex with Amp-Pcp, PDB code: 3ehj
was solved by
D.Albanesi,
P.M.Alzari,
A.Buschiazzo,
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 Crystal Structure of Deskc-H188V in Complex with Amp-Pcp
(pdb code 3ehj). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Deskc-H188V in Complex with Amp-Pcp, PDB code: 3ehj: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 3ehjGo back to Calcium Binding Sites List in 3ehj
Calcium binding site 1 out
of 2 in the Crystal Structure of Deskc-H188V in Complex with Amp-Pcp
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 3ehjGo back to Calcium Binding Sites List in 3ehj
Calcium binding site 2 out
of 2 in the Crystal Structure of Deskc-H188V in Complex with Amp-Pcp
Mono view Stereo pair view
Reference:
D.Albanesi,
M.Martin,
F.Trajtenberg,
M.C.Mansilla,
A.Haouz,
P.M.Alzari,
D.De Mendoza,
A.Buschiazzo.
Structural Plasticity and Catalysis Regulation of A Thermosensor Histidine Kinase Proc.Natl.Acad.Sci.Usa V. 106 16185 2009.
Page generated: Sat Jul 13 09:25:45 2024
ISSN: ISSN 0027-8424 PubMed: 19805278 DOI: 10.1073/PNAS.0906699106 |
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