Magnesium in PDB 4rf3: Crystal Structure of Ketoreductase From Lactobacillus Kefir, Mutant A94F

The structure of Crystal Structure of Ketoreductase From Lactobacillus Kefir, Mutant A94F, PDB code: 4rf3 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)	56.78 / 1.69
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.150, 110.670, 67.610, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 24.1

The binding sites of Magnesium atom in the Crystal Structure of Ketoreductase From Lactobacillus Kefir, Mutant A94F (pdb code 4rf3). 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, Mutant A94F, PDB code: 4rf3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Ketoreductase From Lactobacillus Kefir, Mutant A94F


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, Mutant A94F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:18.1 occ:1.00 O A:HOH403 1.9 15.3 1.0 O A:GLN252 2.0 17.2 1.0 O A:HOH405 2.1 22.9 1.0 O A:HOH402 2.1 31.4 1.0 O A:HOH404 2.2 19.2 1.0 C A:GLN252 3.0 21.9 1.0 OXT A:GLN252 3.2 20.0 1.0 O A:TYR249 4.4 12.3 1.0 CA A:GLN252 4.4 19.9 1.0 O A:HOH455 4.5 17.8 1.0 O A:THR250 4.6 22.2 1.0 N A:GLN252 4.7 18.4 1.0 CG1 A:VAL148 4.8 17.8 1.0 CG A:GLN252 4.9 15.9 1.0 O A:HOH434 4.9 15.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Ketoreductase From Lactobacillus Kefir, Mutant A94F


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, Mutant A94F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:17.0 occ:1.00 O A:HOH408 2.0 16.5 1.0 OD1 A:ASP25 2.1 17.1 1.0 O A:HOH407 2.1 16.6 1.0 O A:HOH409 2.1 19.4 1.0 O A:HOH406 2.2 18.7 1.0 O A:HOH410 2.3 22.2 1.0 CG A:ASP25 3.1 18.4 1.0 OD2 A:ASP25 3.5 17.9 1.0 O A:ASP25 4.0 16.6 1.0 O A:HOH477 4.1 16.5 1.0 O A:ILE51 4.3 15.4 1.0 CB A:ASP25 4.4 14.0 1.0 C A:ASP25 4.5 15.5 1.0 OE1 A:GLU29 4.5 20.3 1.0 CA A:ASP25 4.6 12.8 1.0 CG2 A:ILE51 4.7 12.5 1.0 CB A:GLU29 4.9 15.5 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