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Magnesium in PDB 2quz: Crystal Structure of the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp

Enzymatic activity of Crystal Structure of the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp

All present enzymatic activity of Crystal Structure of the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp:
3.6.5.2;

Protein crystallography data

The structure of Crystal Structure of the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp, PDB code: 2quz was solved by A.Parret, K.Scheffzek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.33 / 1.49
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 92.100, 92.100, 116.300, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 22.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp (pdb code 2quz). 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 the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp, PDB code: 2quz:

Magnesium binding site 1 out of 1 in 2quz

Go back to Magnesium Binding Sites List in 2quz
Magnesium binding site 1 out of 1 in the Crystal Structure of the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp


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 the Activating H-RASK117R Mutant in Costello Syndrome, Bound to Mg-Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg273

b:14.6
occ:1.00
 O3B A:GDP180 2.0 13.1 1.0
O A:HOH371 2.1 14.1 1.0
O A:HOH373 2.1 15.1 1.0
OG A:SER17 2.1 15.1 1.0
O A:HOH378 2.1 19.2 1.0
O A:HOH372 2.1 15.1 1.0
CB A:SER17 3.2 12.9 1.0
PB A:GDP180 3.3 12.8 1.0
O2B A:GDP180 3.5 16.2 1.0
N A:SER17 3.9 12.9 1.0
CA A:SER17 4.1 13.6 1.0
OD2 A:ASP57 4.1 17.7 1.0
O1A A:GDP180 4.1 15.9 1.0
OD1 A:ASP57 4.3 17.8 1.0
O A:ASP33 4.3 28.2 1.0
O1B A:GDP180 4.3 13.9 1.0
O3A A:GDP180 4.3 14.0 1.0
CD2 A:TYR32 4.4 27.5 1.0
O A:PRO34 4.4 28.1 1.0
CA A:PRO34 4.5 28.2 1.0
O A:THR58 4.5 20.3 1.0
CB A:ALA59 4.6 27.1 1.0
PA A:GDP180 4.6 14.3 1.0
CG A:ASP57 4.6 17.3 1.0
O A:ILE36 4.6 26.7 1.0
C A:PRO34 4.7 28.0 1.0
O2A A:GDP180 4.7 15.8 1.0
O A:HOH319 4.8 23.1 1.0
CE2 A:TYR32 4.9 28.6 1.0
CB A:LYS16 5.0 12.7 1.0

Reference:

E.Denayer, A.Parret, M.Chmara, S.Schubbert, A.Vogels, K.Devriendt, J.P.Frijns, V.Rybin, T.J.De Ravel, K.Shannon, J.Cools, K.Scheffzek, E.Legius. Mutation Analysis in Costello Syndrome: Functional and Structural Characterization of the Hras P.LYS117ARG Mutation. Hum.Mutat. V. 29 232 2008.
ISSN: ISSN 1059-7794
PubMed: 17979197
DOI: 10.1002/HUMU.20616
Page generated: Wed Aug 14 03:10:54 2024

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