Magnesium in PDB 2zpu: Crystal Structure of Modified Serine Racemase From S.Pombe.

All present enzymatic activity of Crystal Structure of Modified Serine Racemase From S.Pombe.:
5.1.1.18;

The structure of Crystal Structure of Modified Serine Racemase From S.Pombe., PDB code: 2zpu was solved by M.Goto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.96 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	59.740, 72.990, 65.070, 90.00, 102.41, 90.00
R / Rfree (%)	18.3 / 20.9

The binding sites of Magnesium atom in the Crystal Structure of Modified Serine Racemase From S.Pombe. (pdb code 2zpu). 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 Crystal Structure of Modified Serine Racemase From S.Pombe., PDB code: 2zpu:

Magnesium binding site 1 out of 1 in the Crystal Structure of Modified Serine Racemase From S.Pombe.


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 Modified Serine Racemase From S.Pombe. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg360 b:10.8 occ:1.00 OD1 A:ASP214 2.1 9.2 1.0 O A:HOH362 2.2 6.3 1.0 OE2 A:GLU208 2.2 10.1 1.0 O A:HOH376 2.2 12.0 1.0 O A:GLY212 2.3 11.6 1.0 O A:HOH363 2.3 9.3 1.0 CG A:ASP214 3.1 15.3 1.0 CD A:GLU208 3.2 11.4 1.0 C A:GLY212 3.4 12.7 1.0 OD2 A:ASP214 3.5 11.1 1.0 CG A:GLU208 3.8 10.1 1.0 N A:ASP214 3.9 11.6 1.0 OE1 A:GLU208 4.0 12.2 1.0 O A:ALA237 4.1 10.3 1.0 CA A:GLY212 4.1 13.9 1.0 O A:THR239 4.1 12.3 1.0 N A:GLY215 4.1 11.2 1.0 OG1 A:THR239 4.2 13.1 1.0 CB A:GLU208 4.2 10.9 1.0 CB A:ASP214 4.3 11.0 1.0 N A:ASN213 4.3 11.3 1.0 O A:GLY183 4.4 11.6 1.0 O A:LEU182 4.5 11.0 1.0 CA A:ASN213 4.5 11.7 1.0 CA A:ASP214 4.6 12.0 1.0 C A:ASN213 4.6 12.5 1.0 C A:ASP214 4.9 13.1 1.0 CA A:GLY215 5.0 10.9 1.0

T.Yamauchi, M.Goto, H.Y.Wu, T.Uo, T.Yoshimura, H.Mihara, T.Kurihara, I.Miyahara, K.Hirotsu, N.Esaki. Serine Racemase with Catalytically Active Lysinoalanyl Residue. J.Biochem. V. 145 421 2009.
ISSN: ISSN 0021-924X
PubMed: 19155267
DOI: 10.1093/JB/MVP010