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Fluorine in PDB 2bcj: Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
Enzymatic activity of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
All present enzymatic activity of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits:
2.7.11.15;
2.7.11.15;
Protein crystallography data
The structure of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits, PDB code: 2bcj
was solved by
J.J.G.Tesmer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 46.78 / 3.06 |
| Space group | P 1 21 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 64.918, 129.954, 122.764, 90.00, 95.81, 90.00 |
| R / Rfree (%) | 24.3 / 29.2 |
Other elements in 2bcj:
The structure of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits also contains other interesting chemical elements:
| Magnesium | (Mg) | 1 atom |
| Aluminium | (Al) | 1 atom |
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
(pdb code 2bcj). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits, PDB code: 2bcj:
Jump to Fluorine binding site number: 1; 2; 3; 4;
In total 4 binding sites of Fluorine where determined in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits, PDB code: 2bcj:
Jump to Fluorine binding site number: 1; 2; 3; 4;
Fluorine binding site 1 out of 4 in 2bcj
Go back to
Fluorine Binding Sites List in 2bcj
Fluorine binding site 1 out
of 4 in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits within 5.0Å range:
|
Fluorine binding site 2 out of 4 in 2bcj
Go back to
Fluorine Binding Sites List in 2bcj
Fluorine binding site 2 out
of 4 in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits within 5.0Å range:
|
Fluorine binding site 3 out of 4 in 2bcj
Go back to
Fluorine Binding Sites List in 2bcj
Fluorine binding site 3 out
of 4 in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits within 5.0Å range:
|
Fluorine binding site 4 out of 4 in 2bcj
Go back to
Fluorine Binding Sites List in 2bcj
Fluorine binding site 4 out
of 4 in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits within 5.0Å range:
|
Reference:
V.M.Tesmer,
T.Kawano,
A.Shankaranarayanan,
T.Kozasa,
J.J.G.Tesmer.
Snapshot of Activated G Proteins at the Membrane: the Gq-GRK2-G Complex Science V. 310 1686 2005.
ISSN: ISSN 0036-8075
PubMed: 16339447
DOI: 10.1126/SCIENCE.1118890
Page generated: Wed Jul 31 13:53:19 2024
ISSN: ISSN 0036-8075
PubMed: 16339447
DOI: 10.1126/SCIENCE.1118890
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