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Magnesium in PDB 5dxn: Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2

Enzymatic activity of Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2

All present enzymatic activity of Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2:
2.4.1.15;

Protein crystallography data

The structure of Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2, PDB code: 5dxn 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) 20.60 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.843, 42.672, 80.221, 90.00, 99.46, 90.00
R / Rfree (%) 21.9 / 25.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2 (pdb code 5dxn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2, PDB code: 5dxn:

Magnesium binding site 1 out of 1 in 5dxn

Go back to Magnesium Binding Sites List in 5dxn
Magnesium binding site 1 out of 1 in the Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Aspergillus Fumigatus Trehalose-6-Phosphate Phosphatase Crystal Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:19.2
occ:1.00
OD2 A:ASP24 2.0 19.9 1.0
O A:ASP26 2.0 26.6 1.0
OD1 A:ASP215 2.0 24.1 1.0
O A:HOH437 2.0 23.9 1.0
O A:HOH509 2.1 27.0 1.0
O A:HOH474 2.1 29.4 1.0
CG A:ASP24 2.9 20.6 1.0
CG A:ASP215 3.1 23.7 1.0
C A:ASP26 3.2 24.7 1.0
OD1 A:ASP24 3.3 21.5 1.0
OD2 A:ASP215 3.5 26.7 1.0
OD2 A:ASP219 4.0 21.3 1.0
CA A:ASP26 4.0 24.8 1.0
OD2 A:ASP216 4.1 34.0 1.0
N A:ASP26 4.1 22.2 1.0
OG1 A:THR28 4.1 20.5 1.0
CB A:ASP26 4.2 22.2 1.0
N A:GLY27 4.2 22.1 1.0
CB A:ASP24 4.3 18.4 1.0
O A:HOH620 4.3 38.6 1.0
CB A:ASP215 4.4 20.1 1.0
CA A:GLY27 4.5 22.7 1.0
CG A:ASP216 4.5 29.6 1.0
N A:ASP215 4.5 19.1 1.0
NZ A:LYS188 4.7 34.5 1.0
C A:TYR25 4.7 19.7 1.0
N A:THR28 4.8 20.3 1.0
C A:GLY27 4.8 19.8 1.0
OD1 A:ASP216 4.9 29.5 1.0
CG A:ASP219 4.9 22.8 1.0
N A:ASP216 4.9 18.5 1.0
CA A:ASP215 4.9 18.6 1.0
O A:HOH506 5.0 30.3 1.0
O A:HOH529 5.0 38.3 1.0

Reference:

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
Page generated: Mon Dec 14 20:13:23 2020

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