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Magnesium in PDB 4hxv: Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal IonsEnzymatic activity of Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions
All present enzymatic activity of Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions:
3.1.3.7; Protein crystallography data
The structure of Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions, PDB code: 4hxv
was solved by
K.F.Tarique,
S.A.Abdul Rehman,
S.Gourinath,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4hxv:
The structure of Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions
(pdb code 4hxv). 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 Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions, PDB code: 4hxv: Magnesium binding site 1 out of 1 in 4hxvGo back to Magnesium Binding Sites List in 4hxv
Magnesium binding site 1 out
of 1 in the Crystal Structure of 3'(2'),5'-Bisphosphate NUCLEOTIDASE1 From Entamoeba Histolytica in Complex with Amp and Metal Ions
Mono view Stereo pair view
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.
Page generated: Mon Dec 14 18:51:17 2020
ISSN: ISSN 0907-4449 PubMed: 25004978 DOI: 10.1107/S1399004714010268 |
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