Magnesium in PDB 3imh: Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm

All present enzymatic activity of Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm:
5.1.3.3;

The structure of Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm, PDB code: 3imh was solved by Y.Patskovsky, R.Toro, M.Dickey, S.Chang, J.M.Sauder, S.K.Burley, S.C.Almo, New York Sgx Research Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.76
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	134.683, 134.683, 103.027, 90.00, 90.00, 90.00
R / Rfree (%)	14 / 17

The structure of Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Magnesium atom in the Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm (pdb code 3imh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm, PDB code: 3imh:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm


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 Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg337 b:18.6 occ:1.00 O B:HOH942 2.0 14.4 1.0 O B:HOH510 2.1 18.0 1.0 O B:HOH663 2.1 19.7 1.0 O A:HOH367 2.1 17.2 1.0 O A:HOH876 2.2 15.7 1.0 NE2 A:HIS281 2.3 15.2 1.0 CE1 A:HIS281 3.3 13.2 1.0 CD2 A:HIS281 3.3 14.5 1.0 OD1 B:ASP57 3.8 19.4 1.0 O B:HOH445 4.1 35.4 1.0 OD2 A:ASP292 4.1 16.9 1.0 OD2 B:ASP57 4.2 20.1 1.0 OD1 A:ASP292 4.2 15.3 1.0 O A:HOH491 4.3 33.2 1.0 O B:HOH592 4.3 25.7 1.0 O B:HOH464 4.3 31.6 1.0 ND1 A:HIS281 4.4 14.9 1.0 O A:HOH429 4.4 34.2 1.0 NZ B:LYS60 4.4 47.0 0.5 CG B:ASP57 4.4 19.6 1.0 CG A:HIS281 4.4 11.6 1.0 O A:HOH1023 4.6 50.0 1.0 O A:HOH622 4.6 35.6 1.0 CG A:ASP292 4.6 17.4 1.0 N A:GLY289 4.7 16.7 1.0 CA A:GLY289 4.7 17.9 1.0 NE A:ARG181 4.8 18.6 1.0 CD A:ARG181 4.9 21.4 1.0 OG B:SER54 4.9 24.1 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm


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 Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg338 b:13.9 occ:0.50 O A:HOH551 2.1 29.8 1.0 OD1 A:ASP135 4.3 20.9 1.0 O A:HOH451 4.4 35.1 1.0 O A:GLY132 4.4 14.0 1.0 O A:HOH894 4.7 55.7 1.0 O A:HOH1030 4.7 47.8 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus Ncfm within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg337 b:28.3 occ:1.00 O B:HOH635 2.1 25.2 1.0 O B:HOH552 2.1 22.7 1.0 O B:HOH575 2.1 23.7 1.0 O B:HOH400 2.2 28.8 1.0 NE2 B:HIS281 2.3 19.1 1.0 O B:HOH586 2.3 29.8 1.0 CE1 B:HIS281 3.2 19.3 1.0 CD2 B:HIS281 3.3 18.6 1.0 OD2 B:ASP292 4.1 16.9 1.0 OD1 B:ASP292 4.1 17.5 1.0 O B:HOH1029 4.2 47.8 1.0 ND1 B:HIS281 4.3 19.3 1.0 O B:HOH572 4.4 40.1 1.0 CG B:HIS281 4.4 17.2 1.0 O B:HOH834 4.5 45.6 1.0 CG B:ASP292 4.6 18.4 1.0 NE B:ARG181 4.6 19.3 1.0 CA B:GLY289 4.6 18.1 1.0 N B:GLY289 4.7 14.7 1.0 O B:HOH604 4.8 23.2 1.0 CD B:ARG181 4.8 21.0 1.0

Y.Patskovsky, R.Toro, M.Dickey, S.Chang, J.M.Sauder, S.K.Burley, S.C.Almo. Crystal Structure of Galactose 1-Epimerase From Lactobacillus Acidophilus To Be Published.