Magnesium in PDB 8hx6: Crystal Structure of 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae

All present enzymatic activity of Crystal Structure of 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae:
2.6.1.85;

The structure of Crystal Structure of 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae, PDB code: 8hx6 was solved by Y.Nakamichi, M.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.26 / 2.14
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	98.67, 171.405, 160.838, 90, 90, 90
R / Rfree (%)	22.4 / 27.2

The binding sites of Magnesium atom in the Crystal Structure of 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae (pdb code 8hx6). 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 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae, PDB code: 8hx6:

Magnesium binding site 1 out of 1 in the Crystal Structure of 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae


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 4-Amino-4-Deoxychorismate Synthase From Streptomyces Venezuelae within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg703 b:63.3 occ:1.00 O A:HOH833 2.1 50.7 1.0 OD1 A:ASP175 2.4 51.2 1.0 O A:HOH831 2.4 63.0 1.0 O A:HOH808 2.4 58.9 1.0 O A:SER174 2.7 47.6 1.0 CG A:ASP175 3.5 50.4 1.0 C A:SER174 3.6 48.8 1.0 CA A:ASP175 3.7 48.7 1.0 N A:ASP175 4.0 49.0 1.0 O A:ILE172 4.1 50.6 1.0 CB A:ASP175 4.1 49.5 1.0 OD2 A:ASP175 4.5 51.8 1.0 C A:ASP175 4.9 47.8 1.0 CA A:SER174 4.9 50.1 1.0 N A:SER174 4.9 50.1 1.0

Y.Nakamichi, J.Kobayashi, K.Toyoda, M.Suda, K.Hiraga, M.Inui, M.Watanabe. Structural Basis For the Allosteric Pathway of 4-Amino-4-Deoxychorismate Synthase. Acta Crystallogr D Struct V. 79 895 2023BIOL.
ISSN: ISSN 2059-7983
PubMed: 37712435
DOI: 10.1107/S2059798323006320