Magnesium in PDB 3nc1: Crystal Structure of the CRM1-Rangtp Complex

The structure of Crystal Structure of the CRM1-Rangtp Complex, PDB code: 3nc1 was solved by T.Guttler, T.Madl, P.Neumann, D.Deichsel, L.Corsini, T.Monecke, R.Ficner, M.Sattler, D.Gorlich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.52 / 3.35
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	156.802, 216.158, 123.818, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 25.4

The binding sites of Magnesium atom in the Crystal Structure of the CRM1-Rangtp Complex (pdb code 3nc1). 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 the CRM1-Rangtp Complex, PDB code: 3nc1:

Magnesium binding site 1 out of 1 in the Crystal Structure of the CRM1-Rangtp Complex


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 the CRM1-Rangtp Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg182 b:69.2 occ:1.00 OG1 C:THR24 2.2 0.3 1.0 O1G C:GTP181 2.3 0.4 1.0 O1B C:GTP181 2.3 0.6 1.0 OG1 C:THR42 2.5 1.0 1.0 PG C:GTP181 3.2 0.5 1.0 O3B C:GTP181 3.3 0.2 1.0 PB C:GTP181 3.4 0.7 1.0 OD1 C:ASP65 3.4 0.0 1.0 OD2 C:ASP65 3.4 0.3 1.0 CB C:THR24 3.4 0.8 1.0 CG2 C:THR42 3.4 0.4 1.0 CB C:THR42 3.5 0.5 1.0 N C:THR24 3.7 0.2 1.0 CG C:ASP65 3.8 0.8 1.0 O1A C:GTP181 3.8 0.4 1.0 O2G C:GTP181 3.8 0.5 1.0 O C:THR66 4.0 0.8 1.0 N C:THR42 4.1 0.6 1.0 CA C:THR24 4.1 0.8 1.0 O2A C:GTP181 4.1 0.6 1.0 O3A C:GTP181 4.2 69.5 1.0 PA C:GTP181 4.3 0.8 1.0 CB C:LYS23 4.3 0.5 1.0 CA C:THR42 4.4 0.4 1.0 CG2 C:THR24 4.5 0.2 1.0 O3G C:GTP181 4.5 0.2 1.0 O2B C:GTP181 4.5 0.5 1.0 CE C:LYS23 4.6 0.5 1.0 C C:LYS23 4.6 0.0 1.0 CA C:LYS23 4.9 0.8 1.0

T.Guttler, T.Madl, P.Neumann, D.Deichsel, L.Corsini, T.Monecke, R.Ficner, M.Sattler, D.Gorlich. Nes Consensus Redefined By Structures of Pki-Type and Rev-Type Nuclear Export Signals Bound to CRM1. Nat.Struct.Mol.Biol. V. 17 1367 2010.
ISSN: ISSN 1545-9993
PubMed: 20972448
DOI: 10.1038/NSMB.1931