Magnesium in PDB 4dvg: Crystal Structure of E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas

All present enzymatic activity of Crystal Structure of E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas:
3.6.5.2;

The structure of Crystal Structure of E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas, PDB code: 4dvg was solved by D.E.Bosch, D.P.Siderovski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.67 / 2.60
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	138.564, 138.564, 57.765, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / 25.1

The binding sites of Magnesium atom in the Crystal Structure of E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas (pdb code 4dvg). 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 E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas, PDB code: 4dvg:

Magnesium binding site 1 out of 1 in the Crystal Structure of E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas


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 E. Histolytica FORMIN1 Bound to EHRHO1-Gtpgammas within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:73.6 occ:1.00 O2B A:GSP200 1.8 65.7 1.0 O2G A:GSP200 2.0 56.9 1.0 OG1 A:THR52 2.0 56.6 1.0 OG1 A:THR34 2.0 67.4 1.0 PB A:GSP200 3.0 52.2 1.0 PG A:GSP200 3.1 51.9 1.0 CB A:THR52 3.2 55.4 0.0 CB A:THR34 3.3 64.5 1.0 O3B A:GSP200 3.4 46.5 0.8 N A:THR34 3.8 62.1 1.0 O3G A:GSP200 3.8 49.8 1.0 O2A A:GSP200 3.8 58.6 1.0 N A:THR52 3.8 67.2 1.0 O1B A:GSP200 4.0 56.5 1.0 CA A:THR34 4.0 59.4 1.0 O3A A:GSP200 4.1 42.1 1.0 CA A:THR52 4.1 51.6 1.0 OD2 A:ASP74 4.2 79.0 1.0 CG2 A:THR52 4.2 53.6 1.0 OD1 A:ASP74 4.2 92.4 1.0 PA A:GSP200 4.2 56.8 1.0 O1A A:GSP200 4.4 48.5 1.0 CG2 A:THR34 4.4 65.9 1.0 S1G A:GSP200 4.5 62.0 1.0 CG A:ASP74 4.6 83.8 1.0 O A:VAL50 4.6 71.5 1.0 O A:THR75 4.7 61.4 1.0 CB A:LYS33 4.9 52.3 1.0 C A:PRO51 4.9 66.4 1.0 C A:LYS33 4.9 63.0 1.0

D.E.Bosch, B.Yang, D.P.Siderovski. Entamoeba Histolytica RHO1 Regulates Actin Polymerization Through A Divergent, Diaphanous-Related Formin. Biochemistry V. 51 8791 2012.
ISSN: ISSN 0006-2960
PubMed: 23050667
DOI: 10.1021/BI300954G