Magnesium in PDB 3w3z: Crystal Structure of KAP121P Bound to Rangtp

The structure of Crystal Structure of KAP121P Bound to Rangtp, PDB code: 3w3z was solved by J.Kobayashi, Y.Matsuura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.36 / 2.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	97.750, 97.750, 289.981, 90.00, 90.00, 120.00
R / Rfree (%)	26.1 / 29.8

The binding sites of Magnesium atom in the Crystal Structure of KAP121P Bound to Rangtp (pdb code 3w3z). 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 KAP121P Bound to Rangtp, PDB code: 3w3z:

Magnesium binding site 1 out of 1 in the Crystal Structure of KAP121P Bound to Rangtp


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 KAP121P Bound to Rangtp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg201 b:50.4 occ:1.00 OG1 B:THR24 2.1 78.1 1.0 O2B B:GTP202 2.1 71.1 1.0 O B:HOH302 2.1 51.5 1.0 O2G B:GTP202 2.2 80.1 1.0 OG1 B:THR42 2.2 55.6 1.0 O B:HOH303 2.6 62.1 1.0 CB B:THR42 3.1 63.2 1.0 CB B:THR24 3.3 72.4 1.0 PB B:GTP202 3.4 76.7 1.0 PG B:GTP202 3.4 70.4 1.0 O3B B:GTP202 3.7 64.7 1.0 OD1 B:ASP65 3.7 54.4 1.0 OD2 B:ASP65 3.7 64.5 1.0 N B:THR24 3.8 69.1 1.0 N B:THR42 3.9 70.9 1.0 CG B:ASP65 4.0 61.7 1.0 O3G B:GTP202 4.0 69.7 1.0 CA B:THR42 4.1 68.4 1.0 CA B:THR24 4.1 70.2 1.0 O B:THR66 4.1 71.7 1.0 CG2 B:THR42 4.2 62.0 1.0 CG2 B:THR24 4.3 73.1 1.0 O1B B:GTP202 4.4 58.7 1.0 O2A B:GTP202 4.4 63.0 1.0 O3A B:GTP202 4.5 61.5 1.0 O1G B:GTP202 4.7 0.7 1.0 CB B:LYS23 4.7 67.0 1.0 PA B:GTP202 4.8 73.4 1.0 C B:LYS23 4.9 69.8 1.0 CE B:LYS23 4.9 79.9 1.0 C B:ALA41 4.9 85.5 1.0 O1A B:GTP202 5.0 0.9 1.0 NZ B:LYS23 5.0 86.8 1.0 O B:VAL40 5.0 86.9 1.0

J.Kobayashi, Y.Matsuura. Structural Basis For Cell-Cycle-Dependent Nuclear Import Mediated By the Karyopherin KAP121P. J.Mol.Biol. V. 425 1852 2013.
ISSN: ISSN 0022-2836
PubMed: 23541588
DOI: 10.1016/J.JMB.2013.02.035