Magnesium in PDB 1dtn: Mandelate Racemase Mutant D270N Co-Crystallized with (S)-Atrolactate

All present enzymatic activity of Mandelate Racemase Mutant D270N Co-Crystallized with (S)-Atrolactate:
5.1.2.2;

The structure of Mandelate Racemase Mutant D270N Co-Crystallized with (S)-Atrolactate, PDB code: 1dtn 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 / 2.10
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	125.500, 125.500, 107.300, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Mandelate Racemase Mutant D270N Co-Crystallized with (S)-Atrolactate (pdb code 1dtn). 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 D270N Co-Crystallized with (S)-Atrolactate, PDB code: 1dtn:

Magnesium binding site 1 out of 1 in the Mandelate Racemase Mutant D270N Co-Crystallized with (S)-Atrolactate


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 D270N Co-Crystallized with (S)-Atrolactate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg360 b:30.0 occ:1.00 OE1 A:GLU247 2.0 16.6 1.0 OE2 A:GLU221 2.1 14.3 1.0 O A:HOH401 2.2 26.7 1.0 OD2 A:ASP195 2.4 18.1 1.0 O17 A:APG399 2.5 36.1 1.0 O14 A:APG399 2.5 28.2 1.0 CD A:GLU247 2.8 15.5 1.0 OE2 A:GLU247 3.0 18.7 1.0 CD A:GLU221 3.1 13.0 1.0 C13 A:APG399 3.1 33.0 1.0 CG A:ASP195 3.2 10.3 1.0 C12 A:APG399 3.3 35.0 1.0 OD1 A:ASP195 3.6 18.8 1.0 CG A:GLU221 3.6 8.5 1.0 OE1 A:GLU221 3.9 16.2 1.0 C14 A:APG399 4.0 32.4 1.0 O A:HOH463 4.1 17.9 1.0 O15 A:APG399 4.1 34.0 1.0 OE1 A:GLU222 4.1 25.1 1.0 NZ A:LYS164 4.2 14.7 1.0 CG A:GLU247 4.2 11.9 1.0 CB A:ASP195 4.4 5.0 1.0 C3 A:APG399 4.6 36.2 1.0 CE A:MET268 4.6 9.8 1.0 NE2 A:HIS297 4.7 8.6 1.0 CD2 A:HIS297 4.7 9.4 1.0 CB A:GLU221 4.8 7.5 1.0 OD1 A:ASN197 4.8 39.1 1.0 CE A:LYS164 4.8 13.3 1.0 O A:HOH465 4.9 17.5 1.0 CB A:GLU247 4.9 10.8 1.0 C4 A:APG399 4.9 38.3 1.0 CD A:GLU222 5.0 17.3 1.0

B.Mitra, A.T.Kallarakal, J.W.Kozarich, J.A.Gerlt, J.G.Clifton, G.A.Petsko, G.L.Kenyon. Mechanism of the Reaction Catalyzed By Mandelate Racemase: Importance of Electrophilic Catalysis By Glutamic Acid 317. Biochemistry V. 34 2777 1995.
ISSN: ISSN 0006-2960
PubMed: 7893689
DOI: 10.1021/BI00009A006