Magnesium in PDB 1mdl: Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate

All present enzymatic activity of Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate:
5.1.2.2;

The structure of Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate, PDB code: 1mdl was solved by J.G.Clifton, G.A.Petsko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.85
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	125.320, 125.320, 106.420, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate (pdb code 1mdl). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate, PDB code: 1mdl:

Magnesium binding site 1 out of 1 in the Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mandelate Racemase Mutant K166R Co-Crystallized with (R)-Mandelate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg360 b:5.8 occ:1.00 OE1 A:GLU247 2.0 7.7 1.0 O A:HOH465 2.0 2.3 1.0 OE2 A:GLU221 2.0 3.8 1.0 O11 A:SMN399 2.0 17.1 1.0 OD2 A:ASP195 2.1 1.0 1.0 O8 A:SMN399 2.1 15.4 1.0 C10 A:SMN399 2.8 17.6 1.0 CD A:GLU247 2.8 1.1 1.0 C7 A:SMN399 2.9 12.3 1.0 CG A:ASP195 3.1 9.6 1.0 OE2 A:GLU247 3.1 9.4 1.0 CD A:GLU221 3.2 21.9 1.0 OD1 A:ASP195 3.5 2.0 1.0 O12 A:SMN399 3.9 17.4 1.0 O A:HOH459 4.0 4.6 1.0 CG A:GLU221 4.0 4.8 1.0 OE1 A:GLU221 4.0 5.0 1.0 OD1 A:ASN197 4.1 14.5 1.0 O A:HOH480 4.1 26.4 1.0 NZ A:LYS164 4.1 1.0 1.0 C1 A:SMN399 4.2 11.4 1.0 OE1 A:GLU222 4.2 7.8 1.0 CG A:GLU247 4.2 1.0 1.0 CB A:ASP195 4.4 1.0 1.0 CE A:MET268 4.4 3.1 1.0 CE A:LYS164 4.5 6.9 1.0 CD2 A:HIS297 4.6 1.0 1.0 C6 A:SMN399 4.6 16.4 1.0 NE2 A:HIS297 4.7 1.0 1.0 O A:HOH458 4.9 14.1 1.0 CG A:ASN197 4.9 22.9 1.0 CB A:GLU247 4.9 7.6 1.0

A.T.Kallarakal, B.Mitra, J.W.Kozarich, J.A.Gerlt, J.G.Clifton, G.A.Petsko, G.L.Kenyon. Mechanism of the Reaction Catalyzed By Mandelate Racemase: Structure and Mechanistic Properties of the K166R Mutant. Biochemistry V. 34 2788 1995.
ISSN: ISSN 0006-2960
PubMed: 7893690
DOI: 10.1021/BI00009A007