Magnesium in PDB 4rf5: Crystal Structure of Ketoreductase From Lactobacillus Kefir, E145S Mutant

The structure of Crystal Structure of Ketoreductase From Lactobacillus Kefir, E145S Mutant, PDB code: 4rf5 was solved by Y.Tang, N.Tibrewal, D.Cascio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.56 / 1.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.140, 110.340, 69.560, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 18.3

The binding sites of Magnesium atom in the Crystal Structure of Ketoreductase From Lactobacillus Kefir, E145S Mutant (pdb code 4rf5). 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 Ketoreductase From Lactobacillus Kefir, E145S Mutant, PDB code: 4rf5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Ketoreductase From Lactobacillus Kefir, E145S Mutant


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 Ketoreductase From Lactobacillus Kefir, E145S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:14.6 occ:1.00 O A:HOH467 2.1 24.2 1.0 O A:HOH465 2.1 16.6 1.0 O A:HOH466 2.1 19.7 1.0 O A:GLN252 2.1 16.4 1.0 O A:HOH468 2.1 16.5 1.0 C A:GLN252 3.1 17.3 1.0 OXT A:GLN252 3.4 18.1 1.0 O A:TYR249 4.3 14.0 1.0 O A:HOH434 4.4 27.2 1.0 CA A:GLN252 4.5 16.1 1.0 O A:THR250 4.6 17.8 1.0 CG1 A:VAL148 4.7 18.4 1.0 N A:GLN252 4.7 15.1 1.0 CG A:GLN252 4.9 15.2 1.0 C A:THR250 4.9 18.1 1.0 O A:HOH406 5.0 18.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Ketoreductase From Lactobacillus Kefir, E145S Mutant


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 Ketoreductase From Lactobacillus Kefir, E145S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:17.6 occ:1.00 O A:HOH473 2.0 16.8 1.0 OD1 A:ASP25 2.1 16.8 1.0 O A:HOH474 2.1 16.3 1.0 O A:HOH470 2.1 19.0 1.0 O A:HOH472 2.1 17.5 1.0 O A:HOH471 2.2 19.2 1.0 CG A:ASP25 3.1 21.2 1.0 OD2 A:ASP25 3.5 23.5 1.0 O A:ASP25 4.0 14.1 1.0 O A:HOH475 4.2 18.7 1.0 O A:ILE51 4.4 17.7 1.0 CB A:ASP25 4.4 15.5 1.0 OE1 A:GLU29 4.6 22.8 1.0 C A:ASP25 4.6 13.4 1.0 CA A:ASP25 4.7 13.9 1.0 CG2 A:ILE51 4.7 15.3 1.0 CB A:GLU29 4.9 17.0 1.0

E.L.Noey, N.Tibrewal, G.Jimenez-Oses, S.Osuna, J.Park, C.M.Bond, D.Cascio, J.Liang, X.Zhang, G.W.Huisman, Y.Tang, K.N.Houk. Origins of Stereoselectivity in Evolved Ketoreductases. Proc.Natl.Acad.Sci.Usa V. 112 E7065 2015.
ISSN: ISSN 0027-8424
PubMed: 26644568
DOI: 10.1073/PNAS.1507910112