Magnesium in PDB 1qg4: Canine Gdp-Ran F72Y Mutant

The structure of Canine Gdp-Ran F72Y Mutant, PDB code: 1qg4 was solved by H.M.Kent, M.S.Moore, B.B.Quimby, A.M.E.Baker, A.J.Mccoy, G.A.Murphy, A.H.Corbett, M.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	60.520, 60.170, 61.440, 90.00, 101.77, 90.00
R / Rfree (%)	17.4 / 23.7

The binding sites of Magnesium atom in the Canine Gdp-Ran F72Y Mutant (pdb code 1qg4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Canine Gdp-Ran F72Y Mutant, PDB code: 1qg4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Canine Gdp-Ran F72Y Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Canine Gdp-Ran F72Y Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg221 b:33.5 occ:1.00 O A:HOH317 2.0 28.1 1.0 O A:HOH314 2.1 26.6 1.0 O A:HOH315 2.1 31.0 1.0 O1B A:GDP220 2.2 27.5 1.0 OG1 A:THR24 2.2 33.4 1.0 O A:HOH316 2.3 30.6 1.0 PB A:GDP220 3.3 26.6 1.0 CB A:THR24 3.4 32.2 1.0 O2B A:GDP220 3.4 28.2 1.0 N A:THR24 4.1 30.5 1.0 O3B A:GDP220 4.2 26.1 1.0 OG1 A:THR66 4.2 33.9 1.0 OD2 A:ASP65 4.3 27.4 1.0 CA A:THR24 4.3 30.9 1.0 O2A A:GDP220 4.3 29.0 1.0 O A:THR66 4.3 32.1 1.0 CG2 A:THR24 4.4 31.2 1.0 O3A A:GDP220 4.4 28.3 1.0 OD1 A:ASP65 4.4 30.0 1.0 OE2 A:GLU70 4.5 32.4 1.0 O A:HOH304 4.6 54.2 1.0 CG A:ASP65 4.8 30.6 1.0 PA A:GDP220 4.8 29.4 1.0 NZ A:LYS23 4.8 35.0 1.0 CB A:LYS23 5.0 27.8 1.0

Magnesium binding site 2 out of 2 in the Canine Gdp-Ran F72Y Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Canine Gdp-Ran F72Y Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg221 b:33.2 occ:1.00 O1B B:GDP220 1.7 43.1 1.0 O B:HOH310 2.1 22.4 1.0 O B:HOH308 2.2 18.1 1.0 O B:HOH309 2.2 25.9 1.0 OG1 B:THR24 2.2 27.9 1.0 O B:HOH307 2.2 31.4 1.0 PB B:GDP220 2.9 41.5 1.0 O2B B:GDP220 3.2 39.2 1.0 CB B:THR24 3.2 28.4 1.0 O3B B:GDP220 3.9 20.9 1.0 O3A B:GDP220 3.9 37.0 1.0 N B:THR24 4.1 28.9 1.0 CA B:THR24 4.2 28.9 1.0 CG2 B:THR24 4.3 17.1 1.0 OD2 B:ASP65 4.4 35.9 1.0 O B:THR66 4.4 29.4 1.0 OD1 B:ASP65 4.4 36.3 1.0 O2A B:GDP220 4.5 37.6 1.0 OE2 B:GLU70 4.5 26.1 1.0 PA B:GDP220 4.8 38.7 1.0 OG1 B:THR66 4.8 34.2 1.0 CG B:ASP65 4.9 37.5 1.0 O B:HOH254 5.0 31.8 1.0 CB B:LYS23 5.0 26.4 1.0 O1A B:GDP220 5.0 40.7 1.0 N B:GLY68 5.0 32.2 1.0

H.M.Kent, M.S.Moore, B.B.Quimby, A.M.Baker, A.J.Mccoy, G.A.Murphy, A.H.Corbett, M.Stewart. Engineered Mutants in the Switch II Loop of Ran Define the Contribution Made By Key Residues to the Interaction with Nuclear Transport Factor 2 (NTF2) and the Role of This Interaction in Nuclear Protein Import. J.Mol.Biol. V. 289 565 1999.
ISSN: ISSN 0022-2836
PubMed: 10356329
DOI: 10.1006/JMBI.1999.2775