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Atomistry » Sodium » PDB 6c12-6chk » 6c2h » |
Sodium in PDB 6c2h: Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic CoreEnzymatic activity of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core
All present enzymatic activity of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core:
4.2.1.22; Protein crystallography data
The structure of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core, PDB code: 6c2h
was solved by
C.A.Kreinbring,
Y.Tu,
D.Liu,
G.A.Petsko,
D.Ringe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6c2h:
The structure of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core
(pdb code 6c2h). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core, PDB code: 6c2h: Sodium binding site 1 out of 1 in 6c2hGo back to Sodium Binding Sites List in 6c2h
Sodium binding site 1 out
of 1 in the Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core
Mono view Stereo pair view
Reference:
Y.Tu,
C.A.Kreinbring,
M.Hill,
C.Liu,
G.A.Petsko,
C.D.Mccune,
D.B.Berkowitz,
D.Liu,
D.Ringe.
Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: One Enzymatic Step at A Time. Biochemistry V. 57 3134 2018.
Page generated: Tue Oct 8 06:30:06 2024
ISSN: ISSN 1520-4995 PubMed: 29630349 DOI: 10.1021/ACS.BIOCHEM.8B00092 |
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