Magnesium in PDB 1p7t: Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution

All present enzymatic activity of Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution:
2.3.3.9;

The structure of Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution, PDB code: 1p7t was solved by D.M.Anstrom, K.Kallio, S.J.Remington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.22 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.931, 107.394, 204.974, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution (pdb code 1p7t). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution, PDB code: 1p7t:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1000 b:16.9 occ:1.00 O A:HOH2222 1.8 14.2 1.0 OD2 A:ASP455 2.0 24.6 1.0 O A:HOH2253 2.0 15.8 1.0 OE1 A:GLU427 2.0 16.1 1.0 O3 A:PYR810 2.1 20.7 1.0 O1 A:PYR810 2.3 19.4 1.0 C2 A:PYR810 2.8 20.2 1.0 C1 A:PYR810 3.0 21.0 1.0 CD A:GLU427 3.1 28.6 1.0 CG A:ASP455 3.1 25.7 1.0 CB A:ASP455 3.4 13.1 1.0 OE2 A:GLU427 3.5 18.8 1.0 NH1 A:ARG338 3.9 21.7 1.0 OD2 A:ASP273 4.0 19.1 1.0 CH3 A:ACO800 4.1 30.0 1.0 NZ A:LYS392 4.1 13.1 1.0 O A:ACO800 4.2 27.1 1.0 C3 A:PYR810 4.2 44.0 1.0 O2 A:PYR810 4.2 13.8 1.0 OD1 A:ASP455 4.2 19.1 1.0 CB A:ALA633 4.3 14.3 1.0 CG A:GLU427 4.4 13.9 1.0 C A:ACO800 4.4 31.4 1.0 N A:ASP455 4.4 16.6 1.0 CA A:ASP455 4.6 14.4 1.0 OE1 A:GLU272 4.6 21.6 1.0 CB A:GLU427 4.7 12.8 1.0 CG A:ASP273 4.8 21.8 1.0 CA A:GLY452 4.8 13.5 1.0 CE A:MET425 4.8 10.9 1.0 CZ A:ARG338 5.0 25.7 1.0 O A:GLY452 5.0 14.8 1.0

Magnesium binding site 2 out of 2 in the Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Escherichia Coli Malate Synthase G:Pyruvate:Acetyl- Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1001 b:17.4 occ:1.00 O3 B:PYR910 2.0 26.3 1.0 O B:HOH2230 2.0 21.2 1.0 OD2 B:ASP455 2.0 19.4 1.0 O B:HOH2223 2.0 14.8 1.0 OE1 B:GLU427 2.1 13.7 1.0 O1 B:PYR910 2.2 23.3 1.0 C2 B:PYR910 2.7 32.5 1.0 C1 B:PYR910 2.9 23.7 1.0 CD B:GLU427 3.1 21.8 1.0 CG B:ASP455 3.1 15.8 1.0 CB B:ASP455 3.5 11.0 1.0 OE2 B:GLU427 3.5 19.3 1.0 NH1 B:ARG338 3.8 17.3 1.0 O B:ACO900 3.9 57.4 1.0 OD1 B:ASP455 4.1 18.2 1.0 OD2 B:ASP273 4.1 18.0 1.0 O2 B:PYR910 4.1 21.0 1.0 CH3 B:ACO900 4.1 53.3 1.0 C3 B:PYR910 4.2 32.7 1.0 NZ B:LYS392 4.2 16.2 1.0 CG B:GLU427 4.4 20.0 1.0 C B:ACO900 4.4 57.6 1.0 CB B:ALA633 4.4 13.0 1.0 N B:ASP455 4.5 7.5 1.0 OE1 B:GLU272 4.6 16.2 1.0 CA B:ASP455 4.6 7.7 1.0 CE B:MET425 4.7 22.0 1.0 CB B:GLU427 4.8 17.5 1.0 CA B:GLY452 4.9 15.8 1.0 CZ B:ARG338 4.9 20.0 1.0 CG B:ASP273 4.9 18.4 1.0 O B:GLY452 5.0 12.8 1.0

D.M.Anstrom, K.Kallio, S.J.Remington. Structure of the Escherichia Coli Malate Synthase G:Pyruvate:Acetyl-Coenzyme A Abortive Ternary Complex at 1.95 Angstrom Resolution Protein Sci. V. 12 1822 2003.
ISSN: ISSN 0961-8368
PubMed: 12930982
DOI: 10.1110/PS.03174303