Magnesium in PDB 2f9g: Crystal Structure of FUS3 Phosphorylated on TYR182

All present enzymatic activity of Crystal Structure of FUS3 Phosphorylated on TYR182:
2.7.1.37;

The structure of Crystal Structure of FUS3 Phosphorylated on TYR182, PDB code: 2f9g was solved by R.P.Bhattacharyya, A.Remenyi, M.C.Good, C.J.Bashor, A.M.Falick, W.A.Lim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.811, 62.533, 86.008, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 26

The binding sites of Magnesium atom in the Crystal Structure of FUS3 Phosphorylated on TYR182 (pdb code 2f9g). 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 FUS3 Phosphorylated on TYR182, PDB code: 2f9g:

Magnesium binding site 1 out of 1 in the Crystal Structure of FUS3 Phosphorylated on TYR182


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 Phosphorylated on TYR182 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg600 b:30.1 occ:1.00 O3B A:ADP500 2.0 29.0 1.0 OD2 A:ASP155 2.0 23.3 1.0 O2A A:ADP500 2.0 21.9 1.0 O A:HOH700 2.2 28.9 1.0 OD1 A:ASN142 2.2 19.7 1.0 O A:HOH699 2.2 30.6 1.0 CG A:ASP155 3.1 25.0 1.0 PB A:ADP500 3.2 30.2 1.0 CG A:ASN142 3.2 21.6 1.0 PA A:ADP500 3.2 25.2 1.0 O3A A:ADP500 3.5 27.8 1.0 ND2 A:ASN142 3.6 18.2 1.0 O2B A:ADP500 3.7 31.5 1.0 CB A:ASP155 3.8 23.3 1.0 OD1 A:ASP155 4.0 29.6 1.0 O5' A:ADP500 4.2 26.6 1.0 C5' A:ADP500 4.3 25.0 1.0 O1A A:ADP500 4.4 22.4 1.0 O1B A:ADP500 4.4 31.3 1.0 OG A:SER141 4.5 28.2 1.0 CB A:ASN142 4.5 20.5 1.0 O A:HOH669 4.7 43.9 1.0 O A:SER141 4.8 21.6 1.0 CA A:ASN142 4.8 21.3 1.0 O3' A:ADP500 4.9 31.2 1.0 NH2 A:ARG55 5.0 31.6 1.0 OD2 A:ASP137 5.0 34.3 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