Magnesium in PDB 2f49: Crystal Structure of FUS3 in Complex with A STE5 Peptide

All present enzymatic activity of Crystal Structure of FUS3 in Complex with A STE5 Peptide:
2.7.1.37;

The structure of Crystal Structure of FUS3 in Complex with A STE5 Peptide, PDB code: 2f49 was solved by A.Remenyi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	94.622, 95.210, 101.662, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 23.4

The binding sites of Magnesium atom in the Crystal Structure of FUS3 in Complex with A STE5 Peptide (pdb code 2f49). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of FUS3 in Complex with A STE5 Peptide, PDB code: 2f49:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of FUS3 in Complex with A STE5 Peptide


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 FUS3 in Complex with A STE5 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:44.4 occ:1.00 O A:TYR24 1.9 54.3 1.0 NZ A:LYS49 2.7 43.3 1.0 C A:TYR24 2.8 53.7 1.0 N A:GLU45 2.9 26.0 1.0 CA A:GLY25 3.3 44.5 1.0 N A:GLY25 3.4 49.9 1.0 O A:GLU45 3.5 26.9 1.0 C A:GLU45 3.6 26.6 1.0 CE A:LYS49 3.7 40.9 1.0 CA A:GLU45 3.8 27.7 1.0 CA A:ILE44 3.8 25.1 1.0 C A:ILE44 3.8 24.9 1.0 O A:ALA23 3.9 56.3 1.0 CB A:GLU45 3.9 32.0 1.0 CA A:TYR24 3.9 56.0 1.0 CG2 A:ILE44 4.0 27.2 1.0 N A:PRO46 4.4 26.0 1.0 CB A:ILE44 4.5 25.4 1.0 O A:LYS43 4.5 23.1 1.0 CG A:GLU45 4.6 37.8 1.0 C A:ALA23 4.7 55.9 1.0 C A:GLY25 4.8 41.4 1.0 N A:TYR24 4.8 56.2 1.0 OE1 A:GLU45 5.0 43.6 1.0 CA A:PRO46 5.0 25.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of FUS3 in Complex with A STE5 Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of FUS3 in Complex with A STE5 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:49.9 occ:1.00 O B:TYR24 2.2 57.0 1.0 N B:GLU45 2.8 28.2 1.0 C B:TYR24 3.2 55.6 1.0 NZ B:LYS49 3.3 46.3 1.0 CA B:GLY25 3.4 45.3 1.0 O B:GLU45 3.4 27.4 1.0 C B:GLU45 3.6 28.7 1.0 CA B:GLU45 3.7 28.5 1.0 N B:GLY25 3.7 51.6 1.0 C B:ILE44 3.8 27.6 1.0 CA B:ILE44 3.8 28.1 1.0 CB B:GLU45 3.8 31.6 1.0 CG2 B:ILE44 4.0 32.6 1.0 O B:ALA23 4.0 60.0 1.0 CG B:GLU45 4.2 40.1 1.0 N B:PRO46 4.3 28.1 1.0 CA B:TYR24 4.4 57.9 1.0 CB B:ILE44 4.5 32.1 1.0 O B:LYS43 4.5 26.9 1.0 CE B:LYS49 4.6 42.5 1.0 C B:GLY25 4.9 41.9 1.0 N B:ILE44 4.9 26.8 1.0 O B:ILE44 4.9 25.3 1.0 C B:ALA23 4.9 59.6 1.0 CA B:PRO46 5.0 28.5 1.0

R.P.Bhattacharyya, A.Remenyi, M.C.Good, C.J.Bashor, A.M.Falick, W.A.Lim. The STE5 Scaffold Allosterically Modulates Signaling Output of the Yeast Mating Pathway Science V. 311 822 2006.
ISSN: ISSN 0036-8075
PubMed: 16424299
DOI: 10.1126/SCIENCE.1120941