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Calcium in PDB 6c4p: Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Pmp ComplexEnzymatic activity of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Pmp Complex
All present enzymatic activity of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Pmp Complex:
4.2.1.22; Protein crystallography data
The structure of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Pmp Complex, PDB code: 6c4p
was solved by
C.A.Kreinbring,
Y.Tu,
D.Liu,
D.B.Berkowitz,
G.A.Petsko,
D.Ringe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6c4p:
The structure of Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Pmp Complex 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 Pmp Complex
(pdb code 6c4p). 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 Pmp Complex, PDB code: 6c4p: Calcium binding site 1 out of 1 in 6c4pGo back to Calcium Binding Sites List in 6c4p
Calcium binding site 1 out
of 1 in the Crystal Structures of Cystathionine Beta-Synthase From Saccharomyces Cerevisiae: the Structure of the Pmp Complex
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: Sat Dec 12 06:01:08 2020
ISSN: ISSN 1520-4995 PubMed: 29630349 DOI: 10.1021/ACS.BIOCHEM.8B00092 |
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