Magnesium in PDB 3ip0: Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin

All present enzymatic activity of Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin:
2.7.6.3;

The structure of Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin, PDB code: 3ip0 was solved by J.Blaszczyk, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.20 / 0.89
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	73.470, 37.910, 57.850, 90.00, 117.18, 90.00
R / Rfree (%)	12.8 / 12.8

The structure of Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin (pdb code 3ip0). 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 in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin, PDB code: 3ip0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin


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 in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg161 b:5.3 occ:1.00 OD1 A:ASP95 2.1 5.2 1.0 OD1 A:ASP97 2.1 5.3 1.0 O2A A:APC171 2.1 5.9 1.0 O A:HOH202 2.1 6.2 1.0 O A:HOH201 2.1 5.8 1.0 O2B A:APC171 2.1 5.2 1.0 HOB2 A:APC171 2.1 6.3 1.0 HOA2 A:APC171 2.8 7.1 1.0 CG A:ASP95 3.0 5.0 1.0 CG A:ASP97 3.1 5.1 1.0 PB A:APC171 3.2 5.4 1.0 PA A:APC171 3.2 5.9 1.0 OD2 A:ASP95 3.3 5.4 1.0 HH12 A:ARG82 3.4 9.3 0.4 H3A2 A:APC171 3.5 6.9 1.0 C3A A:APC171 3.5 5.7 1.0 MG A:MG162 3.5 5.4 1.0 OD2 A:ASP97 3.6 5.7 1.0 O5' A:APC171 3.8 6.0 1.0 HH22 A:ARG82 3.9 10.0 0.4 O A:HOH499 3.9 5.4 0.5 O1B A:APC171 4.0 6.5 1.0 O A:HOH264 4.1 14.4 1.0 OE2 A:GLU77 4.2 5.9 1.0 NH1 A:ARG82 4.2 7.7 0.4 HA A:ASP97 4.2 5.6 1.0 O A:LEU96 4.2 5.3 1.0 HH12 A:ARG92 4.3 10.3 0.5 O A:HOH499 4.3 8.6 0.5 H2 A:APC171 4.3 6.8 1.0 HA A:ASP95 4.4 6.1 1.0 O A:HOH501 4.4 7.5 0.6 CB A:ASP95 4.4 5.3 1.0 HH12 A:ARG92 4.4 8.4 0.5 H A:LEU96 4.4 5.8 1.0 O A:HOH216 4.4 7.2 1.0 CB A:ASP97 4.4 5.2 1.0 O3B A:APC171 4.5 5.2 1.0 O1A A:APC171 4.5 6.6 1.0 H3A1 A:APC171 4.6 6.9 1.0 C A:LEU96 4.6 4.8 1.0 HO6A A:HHS182 4.6 8.4 0.6 NH2 A:ARG82 4.6 8.3 0.4 O3G A:APC171 4.6 7.0 1.0 O6A A:HHS182 4.7 6.9 0.6 HH11 A:ARG82 4.7 9.3 0.4 CA A:ASP97 4.7 4.6 1.0 O1G A:APC171 4.7 5.8 1.0 N A:LEU96 4.7 4.8 1.0 HB2 A:ASP95 4.7 6.4 1.0 O A:HOH504 4.7 6.0 0.2 N3 A:APC171 4.8 5.7 1.0 C2 A:APC171 4.8 5.6 1.0 CA A:ASP95 4.8 5.0 1.0 O6A A:HHR181 4.8 4.5 0.5 N A:ASP97 4.8 4.5 1.0 NH1 A:ARG92 4.8 8.5 0.5 HH11 A:ARG92 4.9 10.3 0.5 HB3 A:ASP97 4.9 6.3 1.0 PG A:APC171 4.9 5.4 1.0 CZ A:ARG82 4.9 5.8 0.4 HH11 A:ARG92 5.0 8.4 0.5 NH1 A:ARG92 5.0 7.0 0.5 C A:ASP95 5.0 5.0 1.0 HO6 A:HHR181 5.0 5.5 0.5 HB3 A:ASP95 5.0 6.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of E. Coli Hppk in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin


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 in Complex with Mgampcpp and 6- Hydroxymethylpterin/6-Carboxypterin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg162 b:5.4 occ:1.00 OD2 A:ASP97 2.0 5.7 1.0 O6A A:HHR181 2.0 4.5 0.5 O1G A:APC171 2.1 5.8 1.0 HOB2 A:APC171 2.1 6.3 1.0 O A:HOH203 2.1 6.4 1.0 O6A A:HHS182 2.1 6.9 0.6 O2B A:APC171 2.1 5.2 1.0 OD2 A:ASP95 2.1 5.4 1.0 HO6A A:HHS182 2.4 8.4 0.6 HO6 A:HHR181 2.4 5.5 0.5 CG A:ASP97 3.0 5.1 1.0 CG A:ASP95 3.2 5.0 1.0 PG A:APC171 3.2 5.4 1.0 PB A:APC171 3.2 5.4 1.0 C6A A:HHR181 3.3 4.4 0.5 HH12 A:ARG121 3.3 7.4 1.0 C6 A:HHS182 3.3 6.6 0.6 OD1 A:ASP97 3.3 5.3 1.0 O3B A:APC171 3.3 5.2 1.0 H6A2 A:HHR181 3.4 5.3 0.5 HH12 A:ARG92 3.4 8.4 0.5 MG A:MG161 3.5 5.3 1.0 OD1 A:ASP95 3.6 5.2 1.0 O3G A:APC171 3.9 7.0 1.0 H6A1 A:HHR181 3.9 5.3 0.5 O1B A:APC171 4.0 6.5 1.0 O A:HOH504 4.0 6.0 0.2 O A:HOH205 4.0 6.6 1.0 N5 A:HHS182 4.0 7.3 0.6 N5 A:HHR181 4.1 3.2 0.5 NH1 A:ARG121 4.1 6.1 1.0 NH1 A:ARG92 4.1 7.0 0.5 C6A A:HHS182 4.1 5.9 0.6 O A:HOH504 4.1 7.9 0.2 O6B A:HHS182 4.1 7.2 0.6 HH11 A:ARG92 4.2 8.4 0.5 C6 A:HHR181 4.2 3.9 0.5 HE3 A:MET124 4.2 9.4 0.4 O A:HOH243 4.2 9.5 1.0 HOG3 A:APC171 4.2 8.4 1.0 HH11 A:ARG121 4.3 7.4 1.0 CB A:ASP97 4.3 5.2 1.0 O2G A:APC171 4.4 6.0 1.0 HB2 A:ASP97 4.4 6.3 1.0 NE2 A:HIS115 4.4 6.1 1.0 CB A:ASP95 4.5 5.3 1.0 O A:HOH499 4.5 5.4 0.5 HB3 A:ASP95 4.5 6.4 1.0 HE1 A:MET124 4.6 9.4 0.4 O A:HOH202 4.6 6.2 1.0 O A:HOH219 4.6 8.3 1.0 HB3 A:ASP97 4.6 6.3 1.0 C3A A:APC171 4.7 5.7 1.0 H3A2 A:APC171 4.7 6.9 1.0 HH22 A:ARG121 4.7 9.4 1.0 HE3 A:MET124 4.8 7.1 0.6 HB2 A:ASP95 4.8 6.4 1.0 HOG2 A:APC171 4.8 7.2 1.0 CE A:MET124 4.8 7.8 0.4 O A:HOH499 4.9 8.6 0.5 O2A A:APC171 4.9 5.9 1.0 HE1 A:MET124 5.0 7.1 0.6

J.Blaszczyk, Y.Li, G.Shi, H.Yan, X.Ji. Dynamic Roles of Arginine Residues 82 and 92 of Escherichia Coli 6-Hydroxymethyl-7,8-Dihydroptein Pyrophosphokinase: Crystallographic Studies Biochemistry V. 42 1573 2003.
ISSN: ISSN 0006-2960
PubMed: 12578370
DOI: 10.1021/BI0267994