Magnesium in PDB 5npo: Promiscuous Protein Self-Assembly As A Function of Protein Stability

All present enzymatic activity of Promiscuous Protein Self-Assembly As A Function of Protein Stability:
3.5.2.6;

The structure of Promiscuous Protein Self-Assembly As A Function of Protein Stability, PDB code: 5npo was solved by R.Cohen-Khait, O.Dym, S.Hamer-Rogotner, G.Schreiber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.94 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	66.909, 52.733, 67.944, 90.00, 90.59, 90.00
R / Rfree (%)	19.9 / 25.6

The binding sites of Magnesium atom in the Promiscuous Protein Self-Assembly As A Function of Protein Stability (pdb code 5npo). 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 Promiscuous Protein Self-Assembly As A Function of Protein Stability, PDB code: 5npo:

Magnesium binding site 1 out of 1 in the Promiscuous Protein Self-Assembly As A Function of Protein Stability


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Promiscuous Protein Self-Assembly As A Function of Protein Stability within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg300 b:37.6 occ:1.00 N B:LYS286 3.5 26.5 1.0 NH2 A:ARG61 3.6 26.0 1.0 CB B:ILE285 3.8 24.8 1.0 O B:LYS286 3.9 25.2 1.0 CA B:ILE285 4.0 25.0 1.0 CG2 B:ILE285 4.2 23.4 1.0 C B:ILE285 4.3 25.1 1.0 OE2 A:GLU37 4.3 32.0 1.0 CB B:LYS286 4.3 35.6 1.0 CA B:LYS286 4.3 29.8 1.0 C B:LYS286 4.5 26.3 1.0 CZ A:ARG61 4.8 26.9 1.0 CE3 B:TRP288 4.9 35.4 1.0

R.Cohen-Khait, O.Dym, S.Hamer-Rogotner, G.Schreiber. Promiscuous Protein Binding As A Function of Protein Stability. Structure V. 25 1867 2017.
ISSN: ISSN 1878-4186
PubMed: 29211984
DOI: 10.1016/J.STR.2017.11.002