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Atomistry » Magnesium » PDB 4um5-4uuw » 4ust » |
Magnesium in PDB 4ust: Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and MagnesiumEnzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium
All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium:
4.6.1.1; Protein crystallography data
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium, PDB code: 4ust
was solved by
S.Kleinboelting,
C.Steegborn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ust:
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium 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 Pyrophosphate Resulting From Soaking with Gtp and Magnesium
(pdb code 4ust). 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 Pyrophosphate Resulting From Soaking with Gtp and Magnesium, PDB code: 4ust: Magnesium binding site 1 out of 1 in 4ustGo back to Magnesium Binding Sites List in 4ust
Magnesium binding site 1 out
of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium
Mono view Stereo pair view
Reference:
S.Kleinbolting,
J.Van Den Heuvel,
C.Steegborn.
Structural Analysis of Human Soluble Adenylyl Cyclase and Crystal Structures of Its Nucleotide Complexes - Implications For Cyclase Catalysis and Evolution. Febs J. V. 281 4151 2014.
Page generated: Tue Aug 20 04:59:22 2024
ISSN: ISSN 1742-464X PubMed: 25040695 DOI: 10.1111/FEBS.12913 |
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