Magnesium in PDB 7cwz: Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa

All present enzymatic activity of Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa:
4.1.1.86;

The structure of Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa, PDB code: 7cwz was solved by X.Yu, M.Gong, J.Huang, W.Liu, C.Chen, R.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.85 / 2.97
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	133.314, 133.314, 390.631, 90, 90, 120
R / Rfree (%)	24.3 / 29.4

The binding sites of Magnesium atom in the Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa (pdb code 7cwz). 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 A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa, PDB code: 7cwz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa


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 A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg701 b:87.8 occ:1.00 OD1 A:ASP550 2.4 70.5 1.0 NE2 A:HIS548 2.5 84.4 1.0 NE2 A:HIS526 2.7 82.7 1.0 CD2 A:HIS548 3.1 88.0 1.0 CG A:ASP550 3.1 70.3 1.0 OD2 A:ASP550 3.2 76.4 1.0 CD2 A:HIS526 3.4 80.0 1.0 CE1 A:HIS548 3.7 84.1 1.0 CE1 A:HIS526 3.8 77.4 1.0 CG A:HIS548 4.4 80.5 1.0 CB A:ASP550 4.5 58.6 1.0 ND1 A:HIS548 4.6 80.7 1.0 CG A:HIS526 4.6 73.5 1.0 ND1 A:HIS526 4.7 73.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa


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 A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:58.1 occ:1.00 NE2 B:HIS548 3.0 64.7 1.0 NE2 B:HIS526 3.1 75.2 1.0 OD1 B:ASP550 3.2 70.0 1.0 CD2 B:HIS526 3.5 65.3 1.0 CD2 B:HIS548 3.5 61.2 1.0 CG B:ASP550 3.6 61.3 1.0 CE1 B:HIS548 3.6 65.8 1.0 OD2 B:ASP550 3.8 64.5 1.0 CE1 B:HIS526 4.3 73.5 1.0 CG B:HIS548 4.4 58.1 1.0 ND1 B:HIS548 4.4 61.1 1.0 CB B:ASP550 4.5 54.6 1.0 CG B:HIS526 4.8 63.7 1.0 N B:ASP550 4.9 56.7 1.0

X.Yu, M.Gong, J.Huang, W.Liu, C.Chen, R.Guo. Crystal Structure of A Tyrosine Decarboxylase From Enterococcus Faecalis K392A Mutant in Complex with the Cofactor Plp and L-Dopa To Be Published.