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Atomistry » Zinc » PDB 3udz-3ujp » 3ugq » |
Zinc in PDB 3ugq: Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom ResolutionEnzymatic activity of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution
All present enzymatic activity of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution:
6.1.1.3; Protein crystallography data
The structure of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution, PDB code: 3ugq
was solved by
K.M.Peterson,
J.Ling,
I.Simonovic,
C.Cho,
D.Soll,
M.Simonovic,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ugq:
The structure of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution
(pdb code 3ugq). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution, PDB code: 3ugq: Zinc binding site 1 out of 1 in 3ugqGo back to Zinc Binding Sites List in 3ugq
Zinc binding site 1 out
of 1 in the Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution
Mono view Stereo pair view
Reference:
J.Ling,
K.M.Peterson,
I.Simonovic,
C.Cho,
D.Soll,
M.Simonovic.
Yeast Mitochondrial Threonyl-Trna Synthetase Recognizes Trna Isoacceptors By Distinct Mechanisms and Promotes Cun Codon Reassignment. Proc.Natl.Acad.Sci.Usa V. 109 3281 2012.
Page generated: Sat Oct 26 17:18:44 2024
ISSN: ISSN 0027-8424 PubMed: 22343532 DOI: 10.1073/PNAS.1200109109 |
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