Magnesium in PDB 1tmj: Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution

All present enzymatic activity of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution:
2.7.6.3;

The structure of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution, PDB code: 1tmj 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)	30.00 / 1.45
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	36.132, 46.570, 43.365, 90.00, 110.36, 90.00
R / Rfree (%)	15.5 / 17.4

The structure of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution (pdb code 1tmj). 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 Apo-Hppk(W89A) at 1.45 Angstrom Resolution, PDB code: 1tmj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution


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 Apo-Hppk(W89A) at 1.45 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg161 b:28.2 occ:1.00 O A:HOH258 1.9 26.1 1.0 O A:HOH257 2.0 36.4 1.0 OD1 A:ASP97 2.0 17.7 1.0 O A:HOH215 2.1 22.4 1.0 OD1 A:ASP95 2.1 29.5 1.0 CG A:ASP97 3.0 17.6 1.0 CG A:ASP95 3.1 26.9 1.0 OD2 A:ASP97 3.3 23.1 1.0 MG A:MG162 3.3 27.7 1.0 O A:HOH265 3.3 44.9 1.0 OD2 A:ASP95 3.4 29.6 1.0 O A:HOH244 3.9 43.7 1.0 O A:HOH375 4.0 41.3 1.0 OE2 A:GLU77 4.1 13.6 1.0 CB A:ASP97 4.4 13.7 1.0 O A:LEU96 4.4 16.6 1.0 O A:HOH260 4.4 36.6 1.0 CB A:ASP95 4.5 18.1 1.0 C A:LEU96 4.7 11.1 1.0 O A:HOH298 4.8 45.5 1.0 CA A:ASP97 4.8 11.0 1.0 CE1 A:HIS115 4.8 29.4 1.0 N A:LEU96 4.9 10.5 1.0 N A:ASP97 4.9 11.1 1.0 CA A:ASP95 4.9 13.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution


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 Apo-Hppk(W89A) at 1.45 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg162 b:27.7 occ:1.00 OD2 A:ASP95 1.9 29.6 1.0 O A:HOH258 2.0 26.1 1.0 O A:HOH246 2.1 25.9 1.0 O A:HOH260 2.1 36.6 1.0 OD2 A:ASP97 2.3 23.1 1.0 O A:HOH244 2.4 43.7 1.0 CG A:ASP95 2.9 26.9 1.0 CG A:ASP97 3.3 17.6 1.0 OD1 A:ASP95 3.3 29.5 1.0 MG A:MG161 3.3 28.2 1.0 OD1 A:ASP97 3.5 17.7 1.0 O A:HOH265 3.7 44.9 1.0 NH1 A:ARG121 3.8 30.9 1.0 O A:HOH211 4.1 17.0 1.0 O A:HOH240 4.1 34.8 1.0 O A:HOH282 4.1 28.6 1.0 O A:HOH314 4.1 45.0 1.0 CB A:ASP95 4.2 18.1 1.0 CE A:MET124 4.4 19.3 1.0 CB A:ASP97 4.6 13.7 1.0 O A:HOH257 4.6 36.4 1.0 NE2 A:HIS115 4.6 31.6 1.0 CE1 A:HIS115 4.7 29.4 1.0 CZ A:ARG121 4.9 23.1 1.0

Y.Li, J.Blaszczyk, Y.Wu, G.Shi, X.Ji, H.Yan. Is the Critical Role of Loop 3 of Escherichia Coli 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase in Catalysis Due to Loop-3 Residues Arginine-84 and Tryptophan-89? Site-Directed Mutagenesis, Biochemical, and Crystallographic Studies. Biochemistry V. 44 8590 2005.
ISSN: ISSN 0006-2960
PubMed: 15952765
DOI: 10.1021/BI0503495