Magnesium in PDB 4k6e: Crystal Structure of Saccharomyces Cerevisiae DCP2 Nudix Domain in Complex with Mg

The structure of Crystal Structure of Saccharomyces Cerevisiae DCP2 Nudix Domain in Complex with Mg, PDB code: 4k6e was solved by R.A.Aglietti, S.N.Floor, J.D.Gross, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.53 / 2.10
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	85.054, 85.054, 48.749, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 19.1

The binding sites of Magnesium atom in the Crystal Structure of Saccharomyces Cerevisiae DCP2 Nudix Domain in Complex with Mg (pdb code 4k6e). 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 Saccharomyces Cerevisiae DCP2 Nudix Domain in Complex with Mg, PDB code: 4k6e:

Magnesium binding site 1 out of 1 in the Crystal Structure of Saccharomyces Cerevisiae DCP2 Nudix Domain in Complex with Mg


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 Saccharomyces Cerevisiae DCP2 Nudix Domain in Complex with Mg within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:27.8 occ:1.00 O A:HOH402 2.1 26.7 1.0 OE1 A:GLU149 2.1 31.9 1.0 O A:HOH443 2.1 23.7 1.0 O A:HOH441 2.1 26.0 1.0 O A:HOH444 2.1 25.6 1.0 O A:HOH405 2.1 28.3 1.0 CD A:GLU149 3.1 35.7 1.0 OE2 A:GLU149 3.4 35.6 1.0 OE1 A:GLU152 3.7 33.5 1.0 O A:HOH440 4.0 43.9 1.0 OE2 A:GLU198 4.0 24.2 1.0 CA A:GLY134 4.1 21.2 1.0 OE1 A:GLU198 4.2 27.8 1.0 O A:HOH428 4.4 41.8 1.0 CG A:GLU149 4.4 27.9 1.0 O A:ARG133 4.5 26.6 1.0 CD A:GLU198 4.5 26.1 1.0 CD A:GLU152 4.8 26.4 1.0 OE2 A:GLU153 4.8 20.8 1.0 CB A:GLU149 4.8 23.7 1.0 N A:LYS135 4.9 27.2 1.0 C A:GLY134 5.0 27.2 1.0

R.A.Aglietti, S.N.Floor, C.L.Mcclendon, M.P.Jacobson, J.D.Gross. Active Site Conformational Dynamics Are Coupled to Catalysis in the Mrna Decapping Enzyme DCP2. Structure V. 21 1571 2013.
ISSN: ISSN 0969-2126
PubMed: 23911090
DOI: 10.1016/J.STR.2013.06.021