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Atomistry » Calcium » PDB 4cgt-4cud » 4clk » |
Calcium in PDB 4clk: Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-TriphosphateEnzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate
All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate:
4.6.1.1; Protein crystallography data
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate, PDB code: 4clk
was solved by
S.Kleinboelting,
M.Weyand,
C.Steegborn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4clk:
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate
(pdb code 4clk). 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 Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate, PDB code: 4clk: Calcium binding site 1 out of 1 in 4clkGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate
![]() Mono view ![]() Stereo pair view
Reference:
S.Kleinboelting,
A.Diaz,
S.Moniot,
J.Van Den Heuvel,
M.Weyand,
L.R.Levin,
J.Buck,
C.Steegborn.
Crystal Structures of Human Soluble Adenylyl Cyclase Reveal Mechanisms of Catalysis and of Its Activation Through Bicarbonate. Proc.Natl.Acad.Sci.Usa V. 111 3727 2014.
Page generated: Tue Jul 8 19:14:06 2025
ISSN: ISSN 0027-8424 PubMed: 24567411 DOI: 10.1073/PNAS.1322778111 |
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