Magnesium in PDB 6fch: Crystal Structure of Human Aprt Wild Type in Complex with Prpp and MG2+

All present enzymatic activity of Crystal Structure of Human Aprt Wild Type in Complex with Prpp and MG2+:
2.4.2.7;

The structure of Crystal Structure of Human Aprt Wild Type in Complex with Prpp and MG2+, PDB code: 6fch was solved by P.Nioche, J.Huyet, M.Ozeir, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.33 / 1.45
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	47.260, 47.350, 47.440, 77.02, 69.53, 61.78
R / Rfree (%)	14.1 / 17.6

The binding sites of Magnesium atom in the Crystal Structure of Human Aprt Wild Type in Complex with Prpp and MG2+ (pdb code 6fch). 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 Human Aprt Wild Type in Complex with Prpp and MG2+, PDB code: 6fch:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Aprt Wild Type in Complex with Prpp and MG2+


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 Human Aprt Wild Type in Complex with Prpp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg200 b:15.0 occ:1.00 O3B A:PRP201 2.2 15.6 1.0 O A:HOH332 2.2 17.4 1.0 O3 A:PRP201 2.3 10.5 1.0 O A:HOH312 2.3 11.0 1.0 O1 A:PRP201 2.4 11.1 1.0 O2 A:PRP201 2.4 11.2 1.0 C2 A:PRP201 3.0 10.5 1.0 C3 A:PRP201 3.2 10.3 1.0 O3A A:PRP201 3.2 16.8 1.0 C1 A:PRP201 3.3 11.1 1.0 PB A:PRP201 3.3 16.5 1.0 PA A:PRP201 3.4 14.3 1.0 O A:ASP65 3.7 11.9 1.0 N A:SER66 3.8 10.7 1.0 O2A A:PRP201 4.0 15.8 1.0 O2B A:PRP201 4.0 19.9 1.0 N A:ARG67 4.1 11.5 1.0 C4 A:PRP201 4.1 10.5 1.0 OD1 A:ASP127 4.1 10.7 1.0 O4 A:PRP201 4.2 12.6 1.0 C A:ASP65 4.2 10.8 1.0 OD2 A:ASP127 4.3 9.9 1.0 O A:HOH311 4.3 18.0 1.0 CB A:ARG67 4.4 13.0 1.0 O1B A:PRP201 4.5 18.2 1.0 OD1 A:ASP128 4.5 10.8 1.0 CG A:ASP127 4.6 12.2 1.0 O1A A:PRP201 4.6 16.9 1.0 NZ A:LYS88 4.7 33.4 1.0 NE A:ARG67 4.7 28.4 1.0 CA A:ARG67 4.8 12.2 1.0 CG A:ARG67 4.9 16.7 1.0 CA A:SER66 4.9 10.8 0.5 CA A:SER66 4.9 10.6 0.5 C A:SER66 4.9 12.1 1.0 N A:GLY68 5.0 10.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Aprt Wild Type in Complex with Prpp and MG2+


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 Human Aprt Wild Type in Complex with Prpp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg200 b:13.2 occ:1.00 O B:HOH333 2.2 10.2 1.0 O3B B:PRP201 2.3 13.8 1.0 O B:HOH319 2.3 16.3 1.0 O3 B:PRP201 2.3 10.3 1.0 O1 B:PRP201 2.4 11.5 1.0 O2 B:PRP201 2.4 10.1 1.0 C2 B:PRP201 3.1 10.9 1.0 C3 B:PRP201 3.2 11.0 1.0 O3A B:PRP201 3.3 16.0 1.0 C1 B:PRP201 3.3 11.0 1.0 PB B:PRP201 3.3 14.3 1.0 PA B:PRP201 3.5 13.8 1.0 O B:ASP65 3.7 12.9 1.0 N B:SER66 3.8 10.5 1.0 C4 B:PRP201 4.1 11.5 1.0 O2B B:PRP201 4.1 17.2 1.0 N B:ARG67 4.1 10.6 1.0 O1A B:PRP201 4.1 17.2 1.0 OD1 B:ASP127 4.1 10.6 1.0 C B:ASP65 4.2 11.7 1.0 O4 B:PRP201 4.2 11.8 1.0 OD2 B:ASP127 4.2 9.3 1.0 O B:HOH338 4.3 17.2 1.0 CB B:ARG67 4.5 12.9 1.0 CG B:ARG67 4.5 16.4 1.0 O1B B:PRP201 4.5 18.2 1.0 OD1 B:ASP128 4.5 10.3 1.0 CG B:ASP127 4.6 10.2 1.0 O2A B:PRP201 4.7 16.9 1.0 NZ B:LYS88 4.8 23.3 0.7 CA B:ARG67 4.8 11.2 1.0 CA B:SER66 4.9 9.2 0.5 CA B:SER66 4.9 9.7 0.5 C B:SER66 4.9 10.5 1.0 N B:GLY68 4.9 11.2 1.0

J.Huyet, M.Ozeir, M.C.Burgevin, B.Pinson, F.Chesney, J.M.Remy, A.R.Siddiqi, R.Lupoli, G.Pinon, C.Saint-Marc, J.F.Gibert, R.Morales, I.Ceballos-Picot, R.Barouki, B.Daignan-Fornier, A.Olivier-Bandini, F.Auge, P.Nioche. Structural Insights Into the Forward and Reverse Enzymatic Reactions in Human Adenine Phosphoribosyltransferase. Cell Chem Biol V. 25 666 2018.
ISSN: ESSN 2451-9448
PubMed: 29576532
DOI: 10.1016/J.CHEMBIOL.2018.02.011