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Zinc in PDB 5on3: Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Leucine 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 Leucine 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 Leucine in the Aminoacylation Conformation:
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 Leucine in the Aminoacylation Conformation, PDB code: 5on3 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) 221.55 / 3.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 159.000, 68.700, 227.200, 90.00, 102.80, 90.00
R / Rfree (%) 24.1 / 27.8

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 Leucine in the Aminoacylation Conformation (pdb code 5on3). 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 Quaternary Complex of Mutant T252A of E. Coli Leucyl-Trna Synthetase with Trna(Leu), Leucyl-Adenylate Analogue, and Post-Transfer Editing Analogue of Leucine in the Aminoacylation Conformation, PDB code: 5on3:

Zinc binding site 1 out of 1 in 5on3

Go back to Zinc Binding Sites List in 5on3
Zinc binding site 1 out of 1 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 Leucine in the Aminoacylation Conformation


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 Leucine in the Aminoacylation Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:0.9
occ:1.00
 SG A:CYS176 2.3 0.6 1.0
SG A:CYS179 2.4 0.6 1.0
SG A:CYS159 2.4 0.9 1.0
OD2 A:ASP162 3.0 93.4 1.0
CB A:CYS176 3.3 0.7 1.0
CG2 A:THR181 3.5 0.3 1.0
CB A:CYS159 3.5 0.0 1.0
CB A:CYS179 3.5 0.8 1.0
CG A:ASP162 3.7 91.6 1.0
OD1 A:ASP162 4.1 92.5 1.0
N A:CYS179 4.3 0.7 1.0
CA A:CYS179 4.4 0.8 1.0
NH1 A:ARG178 4.4 0.5 1.0
O A:CYS179 4.6 0.6 1.0
CB A:ASP162 4.6 90.6 1.0
O A:THR181 4.7 0.3 1.0
C A:CYS179 4.7 0.3 1.0
CA A:CYS176 4.8 0.4 1.0
CA A:CYS159 4.9 0.7 1.0
CB A:THR181 4.9 0.2 1.0

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 23:42:18 2024

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