Magnesium in PDB 3k9n: Allosteric Modulation of H-Ras Gtpase

The structure of Allosteric Modulation of H-Ras Gtpase, PDB code: 3k9n was solved by S.Fetics, M.Young, G.Buhrman, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.34 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	38.423, 38.423, 191.749, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 27.7

The structure of Allosteric Modulation of H-Ras Gtpase also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the Allosteric Modulation of H-Ras Gtpase (pdb code 3k9n). 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 Allosteric Modulation of H-Ras Gtpase, PDB code: 3k9n:

Magnesium binding site 1 out of 1 in the Allosteric Modulation of H-Ras Gtpase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Allosteric Modulation of H-Ras Gtpase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg203 b:23.6 occ:1.00 O2G A:GNP201 2.2 31.1 1.0 O2B A:GNP201 2.2 18.7 1.0 OG A:SER17 2.2 21.3 1.0 O A:HOH167 2.3 25.0 1.0 O A:HOH299 2.3 30.9 1.0 O A:HOH171 2.4 24.2 1.0 CB A:SER17 3.2 23.8 1.0 PG A:GNP201 3.4 27.4 1.0 PB A:GNP201 3.4 22.0 1.0 N3B A:GNP201 3.6 22.4 1.0 N A:SER17 4.0 17.8 1.0 OD2 A:ASP57 4.0 35.2 1.0 OD1 A:ASP57 4.1 30.8 1.0 CA A:SER17 4.2 21.4 1.0 O2A A:GNP201 4.2 21.1 1.0 O3G A:GNP201 4.3 29.6 1.0 O3A A:GNP201 4.4 19.6 1.0 O1B A:GNP201 4.5 20.6 1.0 O1G A:GNP201 4.5 29.0 1.0 CG A:ASP57 4.5 32.3 1.0 PA A:GNP201 4.6 24.1 1.0 O A:THR58 4.6 22.4 1.0 O1A A:GNP201 4.7 22.1 1.0 OE2 A:GLU37 4.8 49.9 1.0 CG A:GLU37 4.8 55.1 1.0 CB A:LYS16 4.9 19.7 1.0

G.Buhrman, G.Holzapfel, S.Fetics, C.Mattos. Allosteric Modulation of Ras Positions Q61 For A Direct Role in Catalysis. Proc.Natl.Acad.Sci.Usa V. 107 4931 2010.
ISSN: ISSN 0027-8424
PubMed: 20194776
DOI: 10.1073/PNAS.0912226107