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Atomistry » Calcium » PDB 6bxz-6ckm » 6c2h » |
Calcium 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:
Calcium Binding Sites:
The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Catalytic Core, PDB code: 6c2h: Calcium binding site 1 out of 1 in 6c2hGo back to Calcium Binding Sites List in 6c2h
Calcium 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: Mon Jul 15 17:19:16 2024
ISSN: ISSN 1520-4995 PubMed: 29630349 DOI: 10.1021/ACS.BIOCHEM.8B00092 |
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