Magnesium in PDB 5dxi: Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain

All present enzymatic activity of Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain:
2.4.1.15;

The structure of Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain, PDB code: 5dxi was solved by Y.Miao, R.G.Brennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.43 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.757, 87.200, 139.271, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.2

The structure of Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Magnesium atom in the Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain (pdb code 5dxi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain, PDB code: 5dxi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:25.7 occ:1.00 F2 A:BEF402 2.0 26.9 1.0 OD2 A:ASP230 2.0 26.1 1.0 O A:HOH540 2.0 27.4 1.0 O A:ASP27 2.1 26.2 1.0 O A:HOH531 2.1 28.2 1.0 OD2 A:ASP25 2.1 25.7 1.0 BE A:BEF402 2.9 26.5 1.0 CG A:ASP25 3.0 25.9 1.0 CG A:ASP230 3.1 29.1 1.0 C A:ASP27 3.2 29.4 1.0 OD1 A:ASP25 3.3 27.5 1.0 OD1 A:ASP230 3.5 24.5 1.0 F1 A:BEF402 3.8 28.8 1.0 CA A:ASP27 3.9 26.1 1.0 OD1 A:ASP234 3.9 24.8 1.0 N A:ASP27 4.0 25.1 1.0 CB A:ASP27 4.0 26.1 1.0 OG1 A:THR29 4.0 23.3 1.0 F3 A:BEF402 4.2 26.8 1.0 N A:GLY28 4.3 28.1 1.0 CB A:ASP230 4.4 28.1 1.0 CB A:ASP25 4.4 21.4 1.0 O A:HOH551 4.5 30.4 1.0 N A:ASP230 4.5 25.4 1.0 CB A:ASP231 4.6 27.1 1.0 CA A:GLY28 4.6 25.9 1.0 C A:TYR26 4.6 25.9 1.0 C6P A:TRE403 4.7 30.7 1.0 N A:ASP231 4.7 27.7 1.0 CG A:ASP234 4.8 23.3 1.0 C A:GLY28 4.8 26.9 1.0 N A:THR29 4.9 25.0 1.0 OD2 A:ASP234 4.9 25.7 1.0 CA A:ASP230 4.9 27.6 1.0 CB A:THR29 4.9 26.1 1.0 O A:HOH660 4.9 31.3 1.0 N A:TYR26 4.9 26.9 1.0

Magnesium binding site 2 out of 2 in the Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of C. Albicans Trehalose-6-Phosphate Phosphatase C-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:27.1 occ:1.00 F1 B:BEF402 1.7 26.2 1.0 O B:HOH566 2.0 27.3 1.0 O B:ASP27 2.0 25.1 1.0 OD2 B:ASP230 2.1 26.6 1.0 O B:HOH520 2.1 22.7 1.0 OD2 B:ASP25 2.2 25.7 1.0 BE B:BEF402 2.9 24.4 1.0 CG B:ASP230 3.1 25.0 1.0 CG B:ASP25 3.1 23.1 1.0 C B:ASP27 3.2 25.6 1.0 OD1 B:ASP230 3.4 23.7 1.0 OD1 B:ASP25 3.5 23.2 1.0 F2 B:BEF402 3.8 23.1 1.0 CA B:ASP27 3.8 26.3 1.0 OD1 B:ASP234 3.9 24.8 1.0 N B:ASP27 3.9 25.6 1.0 CB B:ASP27 4.0 26.1 1.0 OG1 B:THR29 4.0 22.8 1.0 F3 B:BEF402 4.2 26.4 1.0 N B:GLY28 4.2 26.3 1.0 CB B:ASP230 4.4 25.2 1.0 CB B:ASP231 4.4 23.9 1.0 N B:ASP230 4.4 23.5 1.0 CB B:ASP25 4.5 24.4 1.0 O B:HOH549 4.5 27.8 1.0 CA B:GLY28 4.5 24.0 1.0 C B:TYR26 4.6 27.9 1.0 C6P B:TRE403 4.7 29.0 1.0 N B:ASP231 4.7 24.6 1.0 C B:GLY28 4.8 25.6 1.0 CA B:ASP230 4.8 26.4 1.0 N B:THR29 4.9 23.6 1.0 CG B:ASP234 4.9 28.6 1.0 N B:TYR26 4.9 23.3 1.0 CB B:THR29 4.9 22.4 1.0

Y.Miao, J.L.Tenor, D.L.Toffaletti, E.J.Washington, J.Liu, W.R.Shadrick, M.A.Schumacher, R.E.Lee, J.R.Perfect, R.G.Brennan. Structures of Trehalose-6-Phosphate Phosphatase From Pathogenic Fungi Reveal the Mechanisms of Substrate Recognition and Catalysis. Proc.Natl.Acad.Sci.Usa V. 113 7148 2016.
ISSN: ESSN 1091-6490
PubMed: 27307435
DOI: 10.1073/PNAS.1601774113