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Atomistry » Magnesium » PDB 2jga-2mse » 2jky » |
Magnesium in PDB 2jky: Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form)Enzymatic activity of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form)
All present enzymatic activity of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form):
2.4.2.8; Protein crystallography data
The structure of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form), PDB code: 2jky
was solved by
L.Moynie,
M.F.Giraud,
A.Breton,
F.Boissier,
B.Daignan-Fornier,
A.Dautant,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form)
(pdb code 2jky). 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 Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form), PDB code: 2jky: Magnesium binding site 1 out of 1 in 2jkyGo back to Magnesium Binding Sites List in 2jky
Magnesium binding site 1 out
of 1 in the Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Guanosine 5'- Monophosphate) (Tetragonal Crystal Form)
Mono view Stereo pair view
Reference:
L.Moynie,
M.F.Giraud,
A.Breton,
F.Boissier,
B.Daignan-Fornier,
A.Dautant.
Functional Significance of Four Successive Glycine Residues in the Pyrophosphate Binding Loop of Fungal 6-Oxopurine Phosphoribosyltransferases. Protein Sci. V. 21 1185 2012.
Page generated: Wed Aug 14 00:49:26 2024
ISSN: ISSN 0961-8368 PubMed: 22610485 DOI: 10.1002/PRO.2098 |
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