Magnesium in PDB 4xvr: H-Ras Y137F

All present enzymatic activity of H-Ras Y137F:
3.6.5.2;

The structure of H-Ras Y137F, PDB code: 4xvr was solved by C.W.Johnson, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.98 / 2.03
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	39.234, 39.234, 157.204, 90.00, 90.00, 120.00
R / Rfree (%)	22.2 / 28.6

The structure of H-Ras Y137F also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the H-Ras Y137F (pdb code 4xvr). 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 H-Ras Y137F, PDB code: 4xvr:

Magnesium binding site 1 out of 1 in the H-Ras Y137F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of H-Ras Y137F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:37.6 occ:1.00 OG A:SER17 1.9 40.6 1.0 O1G A:GNP202 2.0 37.9 1.0 O A:HOH309 2.1 43.0 1.0 O1B A:GNP202 2.1 39.3 1.0 OG1 A:THR35 2.2 45.9 1.0 O A:HOH328 2.4 41.9 1.0 CB A:SER17 2.8 39.5 1.0 CB A:THR35 3.1 46.1 1.0 PG A:GNP202 3.3 44.2 1.0 PB A:GNP202 3.3 40.6 1.0 N3B A:GNP202 3.5 41.1 1.0 N A:SER17 3.5 42.9 1.0 CA A:SER17 3.7 39.0 1.0 OD2 A:ASP57 3.8 44.0 1.0 N A:THR35 3.8 44.6 1.0 OD1 A:ASP57 3.9 45.3 1.0 O2A A:GNP202 4.0 40.6 1.0 CA A:THR35 4.1 45.3 1.0 O3A A:GNP202 4.2 39.0 1.0 CG A:ASP57 4.3 43.8 1.0 O3G A:GNP202 4.3 41.1 1.0 CG2 A:THR35 4.3 42.6 1.0 PA A:GNP202 4.3 43.3 1.0 O1A A:GNP202 4.3 40.0 1.0 O2G A:GNP202 4.4 43.1 1.0 O2B A:GNP202 4.4 36.8 1.0 O A:ASP33 4.4 40.4 1.0 O A:THR58 4.6 45.0 1.0 C A:LYS16 4.7 37.6 1.0 C A:PRO34 4.7 48.6 1.0 CB A:LYS16 4.7 38.3 1.0

P.Y.Ting, C.W.Johnson, C.Fang, X.Cao, T.G.Graeber, C.Mattos, J.Colicelli. Tyrosine Phosphorylation of Ras By Abl Allosterically Enhances Effector Binding. Faseb J. V. 29 3750 2015.
ISSN: ESSN 1530-6860
PubMed: 25999467
DOI: 10.1096/FJ.15-271510