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Atomistry » Magnesium » PDB 3brw-3c5h » 3c16 » |
Magnesium in PDB 3c16: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and CaEnzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca
All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca:
4.6.1.1; Protein crystallography data
The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca, PDB code: 3c16
was solved by
T.-C.Mou,
S.R.Sprang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3c16:
The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca
(pdb code 3c16). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca, PDB code: 3c16: Magnesium binding site 1 out of 1 in 3c16Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca
![]() Mono view ![]() Stereo pair view
Reference:
T.C.Mou,
N.Masada,
D.M.Cooper,
S.R.Sprang.
Structural Basis For Inhibition of Mammalian Adenylyl Cyclase By Calcium. Biochemistry V. 48 3387 2009.
Page generated: Wed Aug 14 09:24:32 2024
ISSN: ISSN 0006-2960 PubMed: 19243146 DOI: 10.1021/BI802122K |
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