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Atomistry » Magnesium » PDB 1g87-1gpm » 1gim » |
Magnesium in PDB 1gim: Crystal Structure of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5)Enzymatic activity of Crystal Structure of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5)
All present enzymatic activity of Crystal Structure of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5):
6.3.4.4; Protein crystallography data
The structure of Crystal Structure of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5), PDB code: 1gim
was solved by
B.W.Poland,
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 Crystal Structure of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5)
(pdb code 1gim). 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 Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5), PDB code: 1gim: Magnesium binding site 1 out of 1 in 1gimGo back to Magnesium Binding Sites List in 1gim
Magnesium binding site 1 out
of 1 in the Crystal Structure of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp, Hadacidin, NO3-, and MG2+. Data Collected at 100K (pH 6.5)
Mono view Stereo pair view
Reference:
B.W.Poland,
H.J.Fromm,
R.B.Honzatko.
Crystal Structures of Adenylosuccinate Synthetase From Escherichia Coli Complexed with Gdp, Imp Hadacidin, NO3-, and MG2+. J.Mol.Biol. V. 264 1013 1996.
Page generated: Mon Dec 14 05:57:50 2020
ISSN: ISSN 0022-2836 PubMed: 9000627 DOI: 10.1006/JMBI.1996.0693 |
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