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Atomistry » Zinc » PDB 3ued-3uk3 » 3uh0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3ued-3uk3 » 3uh0 » |
Zinc in PDB 3uh0: Crystal Structure of the Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl AdenylateEnzymatic activity of Crystal Structure of the Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl Adenylate
All present enzymatic activity of Crystal Structure of the Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl Adenylate:
6.1.1.3; Protein crystallography data
The structure of Crystal Structure of the Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl Adenylate, PDB code: 3uh0
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:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl Adenylate
(pdb code 3uh0). 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 Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl Adenylate, PDB code: 3uh0: Zinc binding site 1 out of 1 in 3uh0Go back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of the Yeast Mitochondrial Threonyl-Trna Synthetase (MST1) in Complex with Threonyl Sulfamoyl Adenylate
![]() 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 17:19:48 2024
ISSN: ISSN 0027-8424 PubMed: 22343532 DOI: 10.1073/PNAS.1200109109 |
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