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Magnesium 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;

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:

Fluorine (F) 4 atoms
Aluminium (Al) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits, PDB code: 2bcj:

Magnesium binding site 1 out of 1 in 2bcj

Go back to Magnesium Binding Sites List in 2bcj
Magnesium binding site 1 out of 1 in the Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-Q and Gbetagamma Subunits


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg 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:
probe atom residue distance (Å) B Occ
Q:Mg361

b:87.7
occ:1.00
O Q:HOH364 1.9 67.3 1.0
O Q:HOH365 2.0 62.2 1.0
F3 Q:ALF362 2.0 83.0 1.0
OG Q:SER53 2.2 91.5 1.0
O2B Q:GDP360 2.2 77.9 1.0
OG1 Q:THR186 2.2 97.1 1.0
CB Q:THR186 2.8 98.6 1.0
O3B Q:GDP360 3.0 76.2 1.0
PB Q:GDP360 3.1 73.0 1.0
CB Q:SER53 3.2 91.8 1.0
F1 Q:ALF362 3.4 83.7 1.0
AL Q:ALF362 3.4 81.7 1.0
N Q:THR186 3.6 98.2 1.0
CA Q:THR186 3.8 98.9 1.0
N Q:SER53 3.8 91.1 1.0
CG2 Q:THR186 3.9 98.1 1.0
OD2 Q:ASP205 4.1 0.8 1.0
CA Q:SER53 4.1 91.8 1.0
O Q:VAL206 4.1 0.1 1.0
OD1 Q:ASP205 4.1 0.2 1.0
O3A Q:GDP360 4.2 74.4 1.0
F2 Q:ALF362 4.2 83.5 1.0
O1B Q:GDP360 4.3 73.7 1.0
O2A Q:GDP360 4.5 73.6 1.0
CG Q:ASP205 4.5 0.0 1.0
O Q:VAL184 4.5 97.1 1.0
O1A Q:GDP360 4.6 71.2 1.0
PA Q:GDP360 4.6 72.6 1.0
O Q:HOH363 4.6 68.2 1.0
NH1 Q:ARG183 4.7 90.0 1.0
C Q:THR186 4.7 99.9 1.0
CB Q:LYS52 4.8 90.0 1.0
O Q:THR186 4.8 100.0 1.0
C Q:PRO185 4.9 97.5 1.0
CE Q:LYS52 4.9 89.0 1.0
C Q:LYS52 4.9 90.5 1.0
C Q:VAL206 5.0 0.3 1.0

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: Mon Dec 14 07:16:28 2020

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