Magnesium in PDB 1ihu: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3

All present enzymatic activity of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3:
3.6.3.16;

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu was solved by T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.15 / 2.15
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	73.897, 75.945, 222.607, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 26.2

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Aluminium	(Al)	1 atom
Cadmium	(Cd)	8 atoms
Arsenic	(As)	1 atom
Chlorine	(Cl)	3 atoms

The binding sites of Magnesium atom in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 (pdb code 1ihu). 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 the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3, PDB code: 1ihu:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3


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 the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg592 b:13.9 occ:1.00 OD1 A:ASP45 1.8 37.5 1.0 O3B A:ADP590 2.1 25.7 1.0 O A:HOH876 2.1 27.3 1.0 OG1 A:THR22 2.1 24.1 1.0 O A:HOH875 2.1 27.9 1.0 O A:HOH877 2.1 27.9 1.0 CG A:ASP45 2.8 40.4 1.0 OD2 A:ASP45 3.2 39.3 1.0 CB A:THR22 3.2 25.8 1.0 PB A:ADP590 3.3 29.3 1.0 O1B A:ADP590 3.5 33.3 1.0 OD2 A:ASP142 4.0 26.3 1.0 N A:THR22 4.0 24.0 1.0 O1A A:ADP590 4.1 32.5 1.0 CB A:ASP45 4.2 28.9 1.0 CA A:THR22 4.2 18.9 1.0 CG2 A:THR22 4.3 25.3 1.0 O3A A:ADP590 4.3 27.1 1.0 O2B A:ADP590 4.4 28.3 1.0 CG A:ASP142 4.6 26.3 1.0 PA A:ADP590 4.6 31.2 1.0 O A:HOH868 4.6 45.8 1.0 O A:HOH747 4.6 35.1 1.0 O A:HOH710 4.6 31.5 1.0 O A:ASP142 4.7 20.2 1.0 NZ A:LYS21 4.8 26.2 1.0 CE A:LYS21 4.9 29.8 1.0 CB A:LYS21 4.9 20.9 1.0 OG1 A:THR502 5.0 34.2 1.0 CB A:ASP142 5.0 25.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3


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 the Escherichia Coli Arsenite-Translocating Atpase in Complex with Mg-Adp-ALF3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg593 b:28.9 occ:1.00 F2 A:AF3700 1.9 49.4 1.0 O3B A:ADP591 2.0 30.8 1.0 O A:HOH878 2.1 31.6 1.0 O A:HOH880 2.1 31.3 1.0 O A:HOH879 2.1 33.1 1.0 OG1 A:THR341 2.2 32.7 1.0 CB A:THR341 3.2 27.8 1.0 PB A:ADP591 3.3 34.9 1.0 AL A:AF3700 3.4 57.4 1.0 O1B A:ADP591 3.5 42.0 1.0 N A:THR341 3.9 30.7 1.0 O1A A:ADP591 3.9 33.8 1.0 OD2 A:ASP447 4.0 31.2 1.0 CA A:THR341 4.1 32.3 1.0 O3A A:ADP591 4.2 34.1 1.0 O A:HOH893 4.2 60.6 1.0 CG2 A:THR341 4.3 24.7 1.0 O A:HOH888 4.4 47.5 1.0 F1 A:AF3700 4.4 60.0 1.0 O2B A:ADP591 4.4 37.9 1.0 CB A:ASP364 4.5 59.9 1.0 PA A:ADP591 4.5 34.2 1.0 OD1 A:ASP364 4.6 57.9 1.0 CG A:ASP447 4.6 34.2 1.0 F3 A:AF3700 4.7 64.4 1.0 O A:ASP447 4.8 30.4 1.0 O A:HOH818 4.9 39.0 1.0 NZ A:LYS340 4.9 26.4 1.0 CG A:ASP364 4.9 65.8 1.0 OG A:SER363 5.0 58.7 1.0 CB A:LYS340 5.0 25.1 1.0 C A:LYS340 5.0 29.2 1.0

T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti. Conformational Changes in Four Regions of the Escherichia Coli Arsa Atpase Link Atp Hydrolysis to Ion Translocation. J.Biol.Chem. V. 276 30414 2001.
ISSN: ISSN 0021-9258
PubMed: 11395509
DOI: 10.1074/JBC.M103671200