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Magnesium in PDB 5c46: Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11

Enzymatic activity of Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11

All present enzymatic activity of Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11:
2.7.1.67;

Protein crystallography data

The structure of Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11, PDB code: 5c46 was solved by J.E.Burke, M.L.Fowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.98 / 2.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.940, 97.950, 190.430, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 24.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11 (pdb code 5c46). 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 An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11, PDB code: 5c46:

Magnesium binding site 1 out of 1 in 5c46

Go back to Magnesium Binding Sites List in 5c46
Magnesium binding site 1 out of 1 in the Crystal Structure of An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11


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 An Engineered Construct of Phosphatidylinositol 4 Kinase III Beta in Complex with Gtp Gamma S Loaded RAB11 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg2001

b:85.2
occ:1.00
 O3G F:GSP2000 2.1 0.1 1.0
OG F:SER25 2.1 66.7 1.0
OG1 F:THR43 2.2 83.7 1.0
O2B F:GSP2000 2.3 64.6 1.0
CB F:SER25 2.9 56.5 1.0
O3B F:GSP2000 3.2 61.7 1.0
PG F:GSP2000 3.2 0.2 1.0
PB F:GSP2000 3.2 55.2 1.0
CB F:THR43 3.4 80.5 1.0
O1A F:GSP2000 3.5 55.8 1.0
N F:THR43 3.7 84.2 1.0
OD2 F:ASP66 3.8 91.2 1.0
O F:LYS41 3.9 88.3 1.0
N F:SER25 4.0 53.7 1.0
CA F:THR43 4.0 81.4 1.0
CA F:SER25 4.1 51.1 1.0
PA F:GSP2000 4.1 57.1 1.0
O2A F:GSP2000 4.1 62.9 1.0
O3A F:GSP2000 4.1 72.8 1.0
S1G F:GSP2000 4.2 0.3 1.0
O2G F:GSP2000 4.3 0.1 1.0
O1B F:GSP2000 4.4 59.0 1.0
OE2 F:GLU47 4.5 91.5 1.0
C F:SER42 4.6 87.5 1.0
CG2 F:THR43 4.6 79.2 1.0
CG F:ASP66 4.7 88.3 1.0
OD1 F:ASP66 4.9 97.7 1.0
OE1 F:GLU47 4.9 92.3 1.0
CA F:SER42 4.9 84.6 1.0
CD F:GLU47 4.9 91.0 1.0

Reference:

M.L.Fowler, J.A.Mcphail, M.L.Jenkins, G.R.Masson, F.U.Rutaganira, K.M.Shokat, R.L.Williams, J.E.Burke. Using Hydrogen Deuterium Exchange Mass Spectrometry to Engineer Optimized Constructs For Crystallization of Protein Complexes: Case Study of PI4KIII Beta with RAB11. Protein Sci. V. 25 826 2016.
ISSN: ESSN 1469-896X
PubMed: 26756197
DOI: 10.1002/PRO.2879
Page generated: Sun Sep 29 01:56:42 2024

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