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Atomistry » Magnesium » PDB 3tx9-3u8u » 3u7g | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 3tx9-3u8u » 3u7g » |
Magnesium in PDB 3u7g: Crystal Structure of Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap)Enzymatic activity of Crystal Structure of Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap)
All present enzymatic activity of Crystal Structure of Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap):
2.7.1.78; 3.1.3.32; Protein crystallography data
The structure of Crystal Structure of Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap), PDB code: 3u7g
was solved by
N.Coquelle,
Z.Havali,
N.Bernstein,
R.Green,
J.N.M.Glover,
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 Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap)
(pdb code 3u7g). 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 Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap), PDB code: 3u7g: Magnesium binding site 1 out of 1 in 3u7gGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of Mpnkp Catalytic Fragment (D170A) Bound to Single- Stranded Dna (Tcctap)
![]() Mono view ![]() Stereo pair view
Reference:
N.Coquelle,
Z.Havali-Shahriari,
N.Bernstein,
R.Green,
J.N.Glover.
Structural Basis For the Phosphatase Activity of Polynucleotide Kinase/Phosphatase on Single- and Double-Stranded Dna Substrates. Proc.Natl.Acad.Sci.Usa V. 108 21022 2011.
Page generated: Mon Aug 11 04:09:09 2025
ISSN: ISSN 0027-8424 PubMed: 22171004 DOI: 10.1073/PNAS.1112036108 |
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