Magnesium in PDB 1u2r: Crystal Structure of Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae

The structure of Crystal Structure of Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae, PDB code: 1u2r was solved by R.Jorgensen, S.P.Yates, J.Nilsson, G.A.Prentice, D.J.Teal, A.R.Merrill, G.R.Andersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	119.725, 151.002, 65.172, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 26.2

The binding sites of Magnesium atom in the Crystal Structure of Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae (pdb code 1u2r). 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 Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae, PDB code: 1u2r:

Magnesium binding site 1 out of 1 in the Crystal Structure of Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae


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 Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg843 b:62.2 occ:1.00 O3B A:GDP1920 2.1 50.8 1.0 OG A:SER33 2.1 50.9 1.0 O2B A:GDP1920 2.3 52.7 1.0 PB A:GDP1920 2.7 50.2 1.0 CB A:SER33 3.1 46.4 1.0 O1A A:GDP1920 3.3 55.6 1.0 O3A A:GDP1920 3.7 52.0 1.0 N A:SER33 3.8 47.0 1.0 O1B A:GDP1920 3.9 49.0 1.0 PA A:GDP1920 3.9 52.4 1.0 CA A:SER33 4.0 47.1 1.0 O A:HOH2035 4.0 51.2 1.0 O2A A:GDP1920 4.5 53.4 1.0 CB A:LYS32 4.9 47.0 1.0 C A:LYS32 4.9 47.9 1.0

R.Jorgensen, S.P.Yates, D.J.Teal, J.Nilsson, G.A.Prentice, A.R.Merrill, G.R.Andersen. Crystal Structure of Adp-Ribosylated Ribosomal Translocase From Saccharomyces Cerevisiae J.Biol.Chem. V. 279 45919 2004.
ISSN: ISSN 0021-9258
PubMed: 15316019
DOI: 10.1074/JBC.M406218200