Magnesium in PDB 5bxq: Structure of the NTF2:Rangdp Complex

The structure of Structure of the NTF2:Rangdp Complex, PDB code: 5bxq was solved by M.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.95 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	155.116, 120.439, 108.836, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 22.5

The binding sites of Magnesium atom in the Structure of the NTF2:Rangdp Complex (pdb code 5bxq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of the NTF2:Rangdp Complex, PDB code: 5bxq:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structure of the NTF2:Rangdp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the NTF2:Rangdp Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg302 b:26.6 occ:1.00 O C:HOH424 2.1 27.6 1.0 O3B C:GDP301 2.1 28.2 1.0 O C:HOH428 2.2 37.2 1.0 O C:HOH435 2.2 23.3 1.0 O C:HOH418 2.2 19.3 1.0 OG1 C:THR24 2.3 27.0 1.0 PB C:GDP301 3.3 28.7 1.0 O2B C:GDP301 3.3 30.6 1.0 CB C:THR24 3.4 25.9 1.0 O B:HOH205 3.5 33.9 1.0 O1B C:GDP301 4.1 28.1 1.0 N C:THR24 4.2 28.6 1.0 OG1 C:THR66 4.2 27.8 1.0 O2A C:GDP301 4.2 27.0 1.0 O C:THR66 4.2 30.5 1.0 O B:HOH231 4.2 38.4 1.0 OD2 C:ASP65 4.2 22.7 1.0 OE2 C:GLU70 4.3 28.7 1.0 CA C:THR24 4.3 27.2 1.0 CG2 C:THR24 4.4 24.1 1.0 OD1 C:ASP65 4.4 21.6 1.0 O3A C:GDP301 4.5 26.9 1.0 PA C:GDP301 4.7 26.0 1.0 O1A C:GDP301 4.7 23.4 1.0 CG C:ASP65 4.7 21.8 1.0 O C:HOH433 4.8 38.0 1.0 NZ C:LYS23 4.9 29.6 1.0 N C:GLY68 4.9 29.2 1.0 CA C:GLY68 5.0 31.9 1.0

Magnesium binding site 2 out of 3 in the Structure of the NTF2:Rangdp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the NTF2:Rangdp Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg302 b:29.2 occ:1.00 O D:HOH425 2.0 28.5 1.0 O D:HOH434 2.0 22.7 1.0 OG1 D:THR24 2.0 32.3 1.0 O D:HOH427 2.2 17.8 1.0 O2B D:GDP301 2.2 27.5 1.0 O D:HOH412 2.2 24.4 1.0 CB D:THR24 3.2 30.6 1.0 PB D:GDP301 3.5 29.9 1.0 O1B D:GDP301 3.7 32.5 1.0 O D:THR66 3.9 27.2 1.0 O A:HOH249 4.0 30.5 1.0 N D:THR24 4.0 26.9 1.0 OD2 D:ASP65 4.1 27.8 1.0 CA D:THR24 4.1 27.9 1.0 OD1 D:ASP65 4.2 28.1 1.0 OG1 D:THR66 4.2 25.4 1.0 O1A D:GDP301 4.2 29.1 1.0 CG2 D:THR24 4.2 31.2 1.0 O3B D:GDP301 4.3 29.6 1.0 OD1 A:ASP94 4.4 34.2 1.0 OE2 D:GLU70 4.4 23.4 1.0 CG D:ASP65 4.5 28.1 1.0 O3A D:GDP301 4.6 30.5 1.0 N D:GLY68 4.7 33.8 1.0 PA D:GDP301 4.8 28.9 1.0 O2A D:GDP301 4.8 28.9 1.0 C D:THR66 4.8 28.4 1.0 CA D:GLY68 4.9 32.1 1.0 O D:HOH416 4.9 29.9 1.0 CB D:LYS23 4.9 25.4 1.0 NZ D:LYS23 4.9 30.4 1.0 CE D:LYS23 5.0 29.5 1.0

Magnesium binding site 3 out of 3 in the Structure of the NTF2:Rangdp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the NTF2:Rangdp Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg301 b:24.6 occ:1.00 O E:HOH421 2.0 19.3 1.0 O E:HOH401 2.1 26.9 1.0 O3B E:GDP303 2.1 27.5 1.0 O E:HOH427 2.1 17.4 1.0 OG1 E:THR24 2.2 22.2 1.0 O E:HOH412 2.2 28.3 1.0 PB E:GDP303 3.2 29.8 1.0 O2B E:GDP303 3.2 33.0 1.0 CB E:THR24 3.3 22.9 1.0 O2A E:GDP303 4.0 26.4 1.0 N E:THR24 4.0 26.6 1.0 O E:HOH443 4.1 55.7 1.0 O1B E:GDP303 4.2 29.1 1.0 OE2 E:GLU70 4.2 37.1 1.0 OG1 E:THR66 4.2 31.5 1.0 CA E:THR24 4.2 25.4 1.0 O E:THR66 4.4 36.0 1.0 CG2 E:THR24 4.4 21.9 1.0 O3A E:GDP303 4.4 35.9 1.0 OD2 E:ASP65 4.4 31.6 1.0 OD1 E:ASP65 4.5 28.5 1.0 PA E:GDP303 4.6 27.3 1.0 O1A E:GDP303 4.8 28.3 1.0 CG E:ASP65 4.9 29.7 1.0 NZ E:LYS23 4.9 33.7 1.0 N E:GLY68 4.9 36.4 1.0 CB E:LYS23 4.9 33.7 1.0 CE E:LYS23 4.9 34.2 1.0 O E:HOH457 5.0 47.2 1.0 CA E:GLY68 5.0 36.9 1.0

M.Stewart, H.M.Kent, A.J.Mccoy. Structural Basis For Molecular Recognition Between Nuclear Transport Factor 2 (NTF2) and the Gdp-Bound Form of the Ras-Family Gtpase Ran. J.Mol.Biol. V. 277 635 1998.
ISSN: ISSN 0022-2836
PubMed: 9533885
DOI: 10.1006/JMBI.1997.1602