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Atomistry » Magnesium » PDB 1ngj-1nn5 » 1nht » |
Magnesium in PDB 1nht: Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100KEnzymatic activity of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K
All present enzymatic activity of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K:
6.3.4.4; Protein crystallography data
The structure of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K, PDB code: 1nht
was solved by
B.W.Poland,
C.A.Bruns,
H.J.Fromm,
R.B.Honzatko,
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 Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K
(pdb code 1nht). 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 Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K, PDB code: 1nht: Magnesium binding site 1 out of 1 in 1nhtGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K
![]() Mono view ![]() Stereo pair view
Reference:
B.W.Poland,
C.Bruns,
H.J.Fromm,
R.B.Honzatko.
Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli. J.Biol.Chem. V. 272 15200 1997.
Page generated: Tue Aug 13 10:04:14 2024
ISSN: ISSN 0021-9258 PubMed: 9182542 DOI: 10.1074/JBC.272.24.15200 |
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