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Magnesium in PDB 4o7i: Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica

Enzymatic activity of Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica

All present enzymatic activity of Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica:
3.1.3.7;

Protein crystallography data

The structure of Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica, PDB code: 4o7i was solved by K.F.Tarique, S.A.A.Rehman, S.Gourinath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.11
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.445, 64.520, 117.184, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 23.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica (pdb code 4o7i). 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 Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica, PDB code: 4o7i:

Magnesium binding site 1 out of 1 in 4o7i

Go back to Magnesium Binding Sites List in 4o7i
Magnesium binding site 1 out of 1 in the Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural and Functional Characterization of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:18.6
occ:1.00
 OE1 A:GLU69 2.0 16.8 1.0
O A:HOH604 2.0 25.5 1.0
O A:HOH603 2.0 20.0 1.0
O A:HOH602 2.1 18.0 1.0
OD1 A:ASP118 2.2 20.5 1.0
O A:ILE120 2.2 14.4 1.0
CG A:ASP118 3.1 17.2 1.0
CD A:GLU69 3.1 18.0 1.0
C A:ILE120 3.2 17.1 1.0
OD2 A:ASP118 3.4 16.6 1.0
OE2 A:GLU69 3.6 20.0 1.0
OG1 A:THR123 3.9 23.2 1.0
O A:HOH522 3.9 16.8 1.0
O A:HOH532 4.0 17.9 1.0
OE2 A:GLU70 4.0 18.7 1.0
N A:ASP121 4.0 19.5 1.0
OD2 A:ASP46 4.0 25.8 1.0
CA A:ASP121 4.1 21.0 1.0
N A:ILE120 4.2 16.3 1.0
CA A:ILE120 4.3 17.5 1.0
CG A:GLU69 4.4 19.1 1.0
O A:HOH543 4.5 38.3 1.0
CB A:ASP118 4.5 15.7 1.0
CB A:GLU69 4.6 16.7 1.0
CD A:PRO119 4.6 13.8 1.0
N A:PRO119 4.8 14.7 1.0
CA A:ASP118 4.8 15.9 1.0
CB A:ILE120 4.8 18.8 1.0
C A:ASP118 4.9 15.8 1.0
N A:GLY122 4.9 18.7 1.0
C A:ASP121 5.0 21.4 1.0

Reference:

K.Faisal Tarique, S.Arif Abdul Rehman, S.Gourinath. Structural Elucidation of A Dual-Activity Pap Phosphatase-1 From Entamoeba Histolytica Capable of Hydrolysing Both 3'-Phosphoadenosine 5'-Phosphate and Inositol 1,4-Bisphosphate Acta Crystallogr.,Sect.D V. 70 2019 2014.
ISSN: ISSN 0907-4449
PubMed: 25004978
DOI: 10.1107/S1399004714010268
Page generated: Mon Dec 14 19:17:00 2020

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