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Atomistry » Magnesium » PDB 4cgk-4cs3 » 4clt » |
Magnesium in PDB 4clt: Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and PyrophosphateEnzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate
All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate:
4.6.1.1; Protein crystallography data
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate, PDB code: 4clt
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 4clt:
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate
(pdb code 4clt). 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 Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate, PDB code: 4clt: Magnesium binding site 1 out of 1 in 4cltGo back to Magnesium Binding Sites List in 4clt
Magnesium binding site 1 out
of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase with Adenosine-3',5'-Cyclic-Monophosphate and Pyrophosphate
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: Thu Aug 15 16:49:13 2024
ISSN: ISSN 0027-8424 PubMed: 24567411 DOI: 10.1073/PNAS.132277811 |
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