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Atomistry » Potassium » PDB 4pkl-4qrh » 4qbt | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 4pkl-4qrh » 4qbt » |
Potassium in PDB 4qbt: Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna SynthetaseEnzymatic activity of Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase
All present enzymatic activity of Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase:
6.1.1.1; Protein crystallography data
The structure of Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase, PDB code: 4qbt
was solved by
S.Mathew,
P.Schimmel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase
(pdb code 4qbt). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase, PDB code: 4qbt: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 4qbtGo back to![]() ![]()
Potassium binding site 1 out
of 2 in the Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase
![]() Mono view ![]() Stereo pair view
Potassium binding site 2 out of 2 in 4qbtGo back to![]() ![]()
Potassium binding site 2 out
of 2 in the Crystal Structure of Tyrosine Bound at the Active Site of Human Tyrosyl Trna Synthetase
![]() Mono view ![]() Stereo pair view
Reference:
M.Sajish,
P.Schimmel.
A Human Trna Synthetase Is A Potent PARP1-Activating Effector Target For Resveratrol Nature 2014.
Page generated: Mon Aug 12 11:53:01 2024
ISSN: ESSN 1476-4687 DOI: 10.1038/NATURE14028 |
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