Zinc »
PDB 5ofa-5on3 »
5on2 »
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
Last articles
Zn in 9JPJZn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
