Magnesium in PDB 3hd2: Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin

All present enzymatic activity of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin:
2.7.6.3;

The structure of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin, PDB code: 3hd2 was solved by J.Blaszczyk, Y.Li, H.Yan, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.96 / 1.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.480, 52.870, 36.700, 90.00, 102.71, 90.00
R / Rfree (%)	15.9 / 18.8

The structure of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin (pdb code 3hd2). 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 E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin, PDB code: 3hd2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin


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 E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg161 b:10.2 occ:1.00 O1A A:APC171 2.1 10.7 1.0 O1B A:APC171 2.1 11.4 1.0 OD1 A:ASP97 2.1 11.1 1.0 OD1 A:ASP95 2.1 10.6 1.0 O A:HOH201 2.1 11.1 1.0 O A:HOH202 2.1 10.4 1.0 CG A:ASP95 3.0 10.9 1.0 CG A:ASP97 3.1 11.0 1.0 PB A:APC171 3.2 11.9 1.0 PA A:APC171 3.3 11.2 1.0 OD2 A:ASP95 3.3 11.4 1.0 MG A:MG162 3.5 11.6 1.0 C3A A:APC171 3.5 11.8 1.0 OD2 A:ASP97 3.5 11.4 1.0 O5' A:APC171 3.8 10.7 1.0 O2B A:APC171 4.0 12.6 1.0 O A:HOH277 4.1 20.3 1.0 OE2 A:GLU77 4.2 9.7 1.0 O A:LEU96 4.2 10.6 1.0 O A:HOH269 4.3 18.1 1.0 NH1 A:ARG92 4.3 14.1 1.0 CB A:ASP95 4.4 11.0 1.0 CB A:ASP97 4.5 10.4 1.0 O3B A:APC171 4.5 12.9 1.0 O A:HOH218 4.5 12.1 1.0 O2A A:APC171 4.6 12.3 1.0 C A:LEU96 4.6 9.7 1.0 N3 A:APC171 4.7 10.9 1.0 C2 A:APC171 4.7 10.3 1.0 N A:LEU96 4.7 9.4 1.0 NH2 A:ARG92 4.7 16.7 1.0 O1G A:APC171 4.7 13.0 1.0 CA A:ASP97 4.7 10.4 1.0 O3G A:APC171 4.7 12.9 1.0 O A:HOH204 4.8 14.5 1.0 CA A:ASP95 4.8 9.7 1.0 N A:ASP97 4.8 9.8 1.0 PG A:APC171 4.9 12.7 1.0 CZ A:ARG92 5.0 14.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin


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 E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg162 b:11.6 occ:1.00 O3G A:APC171 2.1 12.9 1.0 OD2 A:ASP97 2.1 11.4 1.0 OD2 A:ASP95 2.1 11.4 1.0 O A:HOH203 2.1 13.9 1.0 O1B A:APC171 2.1 11.4 1.0 O A:HOH204 2.2 14.5 1.0 CG A:ASP97 3.0 11.0 1.0 CG A:ASP95 3.2 10.9 1.0 PG A:APC171 3.2 12.7 1.0 PB A:APC171 3.2 11.9 1.0 O3B A:APC171 3.3 12.9 1.0 OD1 A:ASP97 3.3 11.1 1.0 MG A:MG161 3.5 10.2 1.0 OD1 A:ASP95 3.6 10.6 1.0 O1G A:APC171 3.9 13.0 1.0 O2B A:APC171 4.0 12.6 1.0 O A:HOH467 4.0 14.9 1.0 NH1 A:ARG121 4.1 13.4 1.0 O A:HOH308 4.3 27.2 1.0 NE2 A:HIS115 4.3 11.1 1.0 O A:HOH345 4.3 33.5 1.0 N4 A:PE0181 4.3 12.8 0.5 CB A:ASP97 4.3 10.4 1.0 O2G A:APC171 4.4 13.2 1.0 C5 A:PE0181 4.4 16.5 0.5 CB A:ASP95 4.4 11.0 1.0 O A:HOH202 4.5 10.4 1.0 O A:HOH477 4.6 22.0 1.0 C3A A:APC171 4.7 11.8 1.0 O A:HOH269 4.7 18.1 1.0 CE A:MET124 4.8 13.0 0.4 O1A A:APC171 4.9 10.7 1.0

J.Blaszczyk, Y.Li, X.Ji, H.Yan. Role of Loop Coupling in Enzymatic Catalysis and Conformational Dynamics To Be Published.