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Atomistry » Magnesium » PDB 1fp6-1g7t » 1fxu » |
Magnesium in PDB 1fxu: Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate IonEnzymatic activity of Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion
All present enzymatic activity of Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion:
2.4.2.1; Protein crystallography data
The structure of Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion, PDB code: 1fxu
was solved by
M.Luic,
A.Bzowska,
D.Shugar,
W.Saenger,
G.Koellner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1fxu:
The structure of Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion
(pdb code 1fxu). 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 Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion, PDB code: 1fxu: Magnesium binding site 1 out of 1 in 1fxuGo back to Magnesium Binding Sites List in 1fxu
Magnesium binding site 1 out
of 1 in the Purine Nucleoside Phosphorylase From Calf Spleen in Complex with N(7)- Acycloguanosine Inhibitor and A Phosphate Ion
Mono view Stereo pair view
Reference:
M.Luic,
G.Koellner,
D.Shugar,
W.Saenger,
A.Bzowska.
Calf Spleen Purine Nucleoside Phosphorylase: Structure of Its Ternary Complex with An N(7)-Acycloguanosine Inhibitor and A Phosphate Anion. Acta Crystallogr.,Sect.D V. 57 30 2001.
Page generated: Tue Aug 13 03:36:17 2024
ISSN: ISSN 0907-4449 PubMed: 11134924 DOI: 10.1107/S0907444900014402 |
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