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Atomistry » Magnesium » PDB 4dhf-4do9 » 4dlg | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 4dhf-4do9 » 4dlg » |
Magnesium in PDB 4dlg: Ternary Structure of the Large Fragment of Taq Dna PolymeraseEnzymatic activity of Ternary Structure of the Large Fragment of Taq Dna Polymerase
All present enzymatic activity of Ternary Structure of the Large Fragment of Taq Dna Polymerase:
2.7.7.7; Protein crystallography data
The structure of Ternary Structure of the Large Fragment of Taq Dna Polymerase, PDB code: 4dlg
was solved by
A.Marx,
K.Diederichs,
S.Obeid,
B.Holzberger,
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 Ternary Structure of the Large Fragment of Taq Dna Polymerase
(pdb code 4dlg). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Ternary Structure of the Large Fragment of Taq Dna Polymerase, PDB code: 4dlg: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 4dlgGo back to Magnesium Binding Sites List in 4dlg
Magnesium binding site 1 out
of 2 in the Ternary Structure of the Large Fragment of Taq Dna Polymerase
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 4dlgGo back to Magnesium Binding Sites List in 4dlg
Magnesium binding site 2 out
of 2 in the Ternary Structure of the Large Fragment of Taq Dna Polymerase
Mono view Stereo pair view
Reference:
B.Holzberger,
S.Obeid,
W.Welte,
K.Diederichs,
A.Marx.
Structural Insights Into the Potential of 4-Fluoroproline to Modulate Biophysical Properties of Protein Chem Sci V. 3 2924 2012.
Page generated: Mon Dec 14 12:36:02 2020
DOI: 10.1039/C2SC20545A |
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