Magnesium in PDB 2fpr: Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.

All present enzymatic activity of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.:
3.1.3.15;

The structure of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model., PDB code: 2fpr was solved by E.S.Rangarajan, M.Cygler, A.Matte, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	53.256, 131.962, 106.140, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 22

The structure of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Bromine	(Br)	7 atoms
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. (pdb code 2fpr). 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 the N-Terminal Domain of E. Coli Hisb. Apo Mg Model., PDB code: 2fpr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:11.9 occ:1.00 OD2 A:ASP10 2.1 9.4 1.0 O A:HOH662 2.1 10.1 1.0 O A:ASP12 2.1 8.7 1.0 O A:HOH675 2.1 9.3 1.0 OD1 A:ASP131 2.1 10.4 1.0 O A:HOH683 2.2 11.7 1.0 CG A:ASP10 3.0 8.8 1.0 CG A:ASP131 3.2 10.4 1.0 C A:ASP12 3.3 8.7 1.0 OD1 A:ASP10 3.4 10.4 1.0 OD2 A:ASP131 3.5 11.2 1.0 O A:HOH549 4.1 13.3 1.0 OG1 A:THR14 4.1 7.8 1.0 CA A:ASP12 4.2 9.2 1.0 O A:HOH519 4.3 10.5 1.0 OD2 A:ASP135 4.3 11.7 1.0 N A:GLY13 4.3 8.6 1.0 CB A:ASP10 4.3 9.5 1.0 N A:ASP12 4.3 8.7 1.0 CD A:ARG132 4.3 13.5 1.0 CG A:ARG132 4.4 11.7 1.0 NE A:ARG132 4.4 15.5 1.0 CA A:GLY13 4.4 8.9 1.0 CB A:ASP12 4.5 9.3 1.0 BR A:BR506 4.5 21.9 1.0 CB A:ASP131 4.5 10.4 1.0 N A:ASP131 4.6 10.0 1.0 OE2 A:GLU18 4.6 18.0 1.0 C A:GLY13 4.7 8.6 1.0 N A:THR14 4.8 8.2 1.0 N A:ARG132 4.9 11.7 1.0 CA A:ASP131 5.0 10.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg504 b:9.1 occ:1.00 OD2 B:ASP10 2.0 7.7 1.0 OD1 B:ASP131 2.1 8.8 1.0 O B:HOH778 2.1 8.1 1.0 O B:HOH780 2.1 11.0 1.0 O B:HOH772 2.1 9.3 1.0 O B:ASP12 2.1 7.9 1.0 CG B:ASP10 3.0 8.4 1.0 CG B:ASP131 3.1 9.3 1.0 C B:ASP12 3.4 7.5 1.0 OD1 B:ASP10 3.4 8.4 1.0 OD2 B:ASP131 3.5 11.3 1.0 OG1 B:THR14 4.1 6.6 1.0 OD2 B:ASP135 4.2 12.1 1.0 N B:GLY13 4.3 6.8 1.0 CA B:GLY13 4.3 7.2 1.0 CG B:ARG132 4.3 13.7 1.0 O B:HOH518 4.3 11.1 1.0 CB B:ASP10 4.3 7.5 1.0 CA B:ASP12 4.3 7.6 1.0 O B:HOH529 4.3 15.8 1.0 NE B:ARG132 4.3 18.1 1.0 CD B:ARG132 4.4 15.6 1.0 N B:ASP131 4.5 9.1 1.0 CB B:ASP131 4.5 9.5 1.0 CB B:ASP12 4.5 7.5 1.0 OE1 B:GLU18 4.5 11.5 1.0 N B:ASP12 4.5 7.6 1.0 C B:GLY13 4.6 6.9 1.0 BR B:BR507 4.6 21.1 1.0 N B:THR14 4.8 6.7 1.0 CA B:ASP131 4.9 9.4 1.0 N B:ARG132 4.9 10.2 1.0 CD B:GLU18 4.9 11.6 1.0

E.S.Rangarajan, A.Proteau, J.Wagner, M.N.Hung, A.Matte, M.Cygler. Structural Snapshots of Escherichia Coli Histidinol Phosphate Phosphatase Along the Reaction Pathway. J.Biol.Chem. V. 281 37930 2006.
ISSN: ISSN 0021-9258
PubMed: 16966333
DOI: 10.1074/JBC.M604916200