Magnesium in PDB 1x1r: Crystal Structure of M-Ras in Complex with Gdp

The structure of Crystal Structure of M-Ras in Complex with Gdp, PDB code: 1x1r was solved by M.Ye, F.Shima, S.Muraoka, J.Liao, H.Okamoto, M.Yamamoto, A.Tamura, N.Yagi, T.Ueki, T.Kataoka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.44 / 1.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.899, 70.668, 43.422, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 20

The binding sites of Magnesium atom in the Crystal Structure of M-Ras in Complex with Gdp (pdb code 1x1r). 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 M-Ras in Complex with Gdp, PDB code: 1x1r:

Magnesium binding site 1 out of 1 in the Crystal Structure of M-Ras in Complex with 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 M-Ras in Complex with Gdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1180 b:5.2 occ:1.00 O2B A:GDP1179 2.0 4.2 1.0 O A:HOH1181 2.0 6.2 1.0 O A:HOH1182 2.1 6.2 1.0 OG A:SER27 2.1 5.4 1.0 O A:HOH1183 2.1 6.0 1.0 O A:HOH1184 2.1 5.7 1.0 CB A:SER27 3.2 5.5 1.0 PB A:GDP1179 3.3 4.3 1.0 O3B A:GDP1179 3.5 4.7 1.0 N A:SER27 3.9 4.3 1.0 CA A:SER27 4.1 5.4 1.0 OD2 A:ASP67 4.1 8.2 1.0 O1A A:GDP1179 4.1 6.1 1.0 O A:ASP43 4.2 10.4 1.0 O A:PRO44 4.2 9.4 1.0 OD1 A:ASP67 4.2 7.7 1.0 O3A A:GDP1179 4.3 5.0 1.0 O1B A:GDP1179 4.3 3.5 1.0 CB A:ALA69 4.4 7.8 1.0 O A:THR68 4.5 5.5 1.0 CD2 A:TYR42 4.5 10.3 1.0 O A:ILE46 4.5 8.8 1.0 PA A:GDP1179 4.6 5.7 1.0 CG A:ASP67 4.6 6.5 1.0 C A:PRO44 4.6 9.8 1.0 CA A:PRO44 4.6 10.7 1.0 O2A A:GDP1179 4.8 7.2 1.0 O A:HOH1206 4.9 14.0 1.0 O A:HOH1202 5.0 11.4 1.0

M.Ye, F.Shima, S.Muraoka, J.Liao, H.Okamoto, M.Yamamoto, A.Tamura, N.Yagi, T.Ueki, T.Kataoka. Crystal Structure of M-Ras Reveals A Gtp-Bound "Off" State Conformation of Ras Family Small Gtpases J.Biol.Chem. V. 280 31267 2005.
ISSN: ISSN 0021-9258
PubMed: 15994326
DOI: 10.1074/JBC.M505503200