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Magnesium in PDB 5dx9: Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans

Enzymatic activity of Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans

All present enzymatic activity of Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans:
2.4.1.15;

Protein crystallography data

The structure of Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans, PDB code: 5dx9 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) 43.31 / 2.15
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 63.074, 63.074, 284.315, 90.00, 90.00, 120.00
R / Rfree (%) 23 / 26.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans (pdb code 5dx9). 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 Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans, PDB code: 5dx9:

Magnesium binding site 1 out of 1 in 5dx9

Go back to Magnesium Binding Sites List in 5dx9
Magnesium binding site 1 out of 1 in the Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Trehalose-6-Phosphate Phosphatase From Cryptococcus Neoformans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:46.5
occ:1.00
O14 A:T6P402 1.9 42.7 1.0
O A:HOH514 2.1 40.5 1.0
OD1 A:ASN24 2.1 40.9 1.0
O A:HOH523 2.1 41.0 1.0
O A:ASP26 2.2 41.4 1.0
OD1 A:ASP210 2.2 42.0 1.0
CG A:ASN24 3.0 40.4 1.0
CG A:ASP210 3.3 44.0 1.0
P1 A:T6P402 3.3 44.4 1.0
C A:ASP26 3.3 41.9 1.0
ND2 A:ASN24 3.4 40.6 1.0
OD2 A:ASP210 3.7 44.6 1.0
OD1 A:ASP214 3.9 40.5 1.0
H23 A:T6P402 3.9 53.0 1.0
O13 A:T6P402 4.0 44.2 1.0
CA A:ASP26 4.0 42.3 1.0
N A:ASP26 4.0 42.0 1.0
O12 A:T6P402 4.0 44.1 1.0
CB A:ASP26 4.0 40.3 1.0
H22 A:T6P402 4.2 52.9 1.0
OG1 A:THR28 4.3 40.4 1.0
CB A:ASN24 4.4 42.5 1.0
N A:GLY27 4.4 40.8 1.0
O11 A:T6P402 4.4 46.7 1.0
CB A:ASP211 4.5 44.3 1.0
N A:ASP210 4.5 41.0 1.0
CB A:ASP210 4.6 41.1 1.0
H17 A:T6P402 4.6 53.8 1.0
N A:ASP211 4.7 41.5 1.0
C A:TYR25 4.7 42.1 1.0
CA A:GLY27 4.7 42.1 1.0
N A:TYR25 4.8 44.8 1.0
CG A:ASP214 4.9 39.3 1.0
NZ A:LYS188 4.9 44.1 1.0
N A:THR28 4.9 42.2 1.0
OD2 A:ASP214 5.0 40.4 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: Sun Sep 29 03:26:30 2024

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