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Atomistry » Potassium » PDB 5irf-5koe » 5kfx | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 5irf-5koe » 5kfx » |
Potassium in PDB 5kfx: Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300SEnzymatic activity of Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S
All present enzymatic activity of Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S:
2.7.7.7; Protein crystallography data
The structure of Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S, PDB code: 5kfx
was solved by
Y.Gao,
W.Yang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5kfx:
The structure of Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S
(pdb code 5kfx). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S, PDB code: 5kfx: Potassium binding site 1 out of 1 in 5kfxGo back to![]() ![]()
Potassium binding site 1 out
of 1 in the Human Dna Polymerase Eta R61A-Dna Ternary Complex: Reaction with 1 Mm MG2+ For 300S
![]() Mono view ![]() Stereo pair view
Reference:
Y.Gao,
W.Yang.
Capture of A Third MG2+ Is Essential For Catalyzing Dna Synthesis. Science V. 352 1334 2016.
Page generated: Sat Aug 9 09:22:12 2025
ISSN: ESSN 1095-9203 PubMed: 27284197 DOI: 10.1126/SCIENCE.AAD9633 |
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