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Zinc in PDB 5on2: Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation
Enzymatic activity of Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation
All present enzymatic activity of Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation:
6.1.1.4;
6.1.1.4;
Protein crystallography data
The structure of Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation, PDB code: 5on2
was solved by
A.Palencia,
S.Cusack,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 50.00 / 3.10 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 159.650, 70.620, 230.340, 90.00, 104.52, 90.00 |
| R / Rfree (%) | 22.6 / 26.3 |
Other elements in 5on2:
The structure of Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation also contains other interesting chemical elements:
| Magnesium | (Mg) | 2 atoms |
Zinc Binding Sites:
The binding sites of Zinc atom in the Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation
(pdb code 5on2). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation, PDB code: 5on2:
Jump to Zinc binding site number: 1; 2;
In total 2 binding sites of Zinc where determined in the Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation, PDB code: 5on2:
Jump to Zinc binding site number: 1; 2;
Zinc binding site 1 out of 2 in 5on2
Go back to
Zinc Binding Sites List in 5on2
Zinc binding site 1 out
of 2 in the Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation within 5.0Å range:
|
Zinc binding site 2 out of 2 in 5on2
Go back to
Zinc Binding Sites List in 5on2
Zinc binding site 2 out
of 2 in the Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Norvaline in the Aminoacylation Conformation within 5.0Å range:
|
Reference:
M.Dulic,
N.Cvetesic,
I.Zivkovic,
A.Palencia,
S.Cusack,
B.Bertosa,
I.Gruic-Sovulj.
Kinetic Origin of Substrate Specificity in Post-Transfer Editing By Leucyl-Trna Synthetase. J. Mol. Biol. V. 430 1 2018.
ISSN: ESSN 1089-8638
PubMed: 29111343
DOI: 10.1016/J.JMB.2017.10.024
Page generated: Sun Oct 27 23:42:19 2024
ISSN: ESSN 1089-8638
PubMed: 29111343
DOI: 10.1016/J.JMB.2017.10.024
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