Magnesium in PDB 5hsi: Crystal Structure of Tyrosine Decarboxylase at 1.73 Angstroms Resolution

All present enzymatic activity of Crystal Structure of Tyrosine Decarboxylase at 1.73 Angstroms Resolution:
4.1.1.25;

The structure of Crystal Structure of Tyrosine Decarboxylase at 1.73 Angstroms Resolution, PDB code: 5hsi was solved by Y.Ni, J.Zhou, H.Zhu, K.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.93 / 1.73
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.787, 126.169, 82.728, 90.00, 109.89, 90.00
R / Rfree (%)	15.5 / 19.1

The binding sites of Magnesium atom in the Crystal Structure of Tyrosine Decarboxylase at 1.73 Angstroms Resolution (pdb code 5hsi). 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 Tyrosine Decarboxylase at 1.73 Angstroms Resolution, PDB code: 5hsi:

Magnesium binding site 1 out of 1 in the Crystal Structure of Tyrosine Decarboxylase at 1.73 Angstroms Resolution


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 Tyrosine Decarboxylase at 1.73 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:23.8 occ:1.00 O B:HOH1148 2.0 24.4 1.0 O B:HOH1387 2.0 30.6 1.0 O B:HOH829 2.2 27.3 1.0 O B:GLY146 4.1 19.8 1.0 OD2 B:ASP381 4.1 23.1 1.0 O B:HOH1153 4.1 34.8 1.0 O B:HOH1168 4.2 29.1 1.0 OD1 B:ASP148 4.3 30.8 1.0 O B:HOH1163 4.3 31.9 1.0 OD2 B:ASP148 4.3 33.8 1.0 O B:HOH1232 4.6 21.3 1.0 CG B:ASP148 4.7 29.9 1.0 O B:HOH1118 4.8 29.9 1.0 O B:HOH1009 4.8 26.8 1.0 C B:GLY146 4.9 22.3 1.0 CA B:GLY146 4.9 18.7 1.0

H.Zhu, G.Xu, K.Zhang, X.Kong, R.Han, J.Zhou, Y.Ni. Crystal Structure of Tyrosine Decarboxylase and Identification of Key Residues Involved in Conformational Swing and Substrate Binding Sci Rep V. 6 27779 2016.
ISSN: ESSN 2045-2322
PubMed: 27292129
DOI: 10.1038/SREP27779