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Magnesium in PDB 5omw: Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation

Enzymatic activity of Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation

All present enzymatic activity of Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation:
6.1.1.4;

Protein crystallography data

The structure of Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation, PDB code: 5omw 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) 220.62 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.250, 68.910, 228.330, 90.00, 104.93, 90.00
R / Rfree (%) 21.9 / 26.4

Other elements in 5omw:

The structure of Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation (pdb code 5omw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation, PDB code: 5omw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5omw

Go back to Magnesium Binding Sites List in 5omw
Magnesium binding site 1 out of 2 in the Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg101

b:47.1
occ:1.00
OP1 B:U8 2.4 30.5 1.0
OP2 B:G9 2.5 31.8 1.0
OP2 B:G12 3.6 27.8 1.0
P B:U8 3.6 31.1 1.0
OP1 B:U11 3.7 31.9 1.0
P B:G9 3.9 31.6 1.0
OP2 B:U8 3.9 30.9 1.0
O5' B:U8 4.4 31.1 1.0
OP2 B:U11 4.5 31.4 1.0
O5' B:G9 4.5 30.7 1.0
C5' B:G9 4.6 30.3 1.0
P B:U11 4.6 32.6 1.0
P B:G12 4.7 27.1 1.0
OP1 B:G9 4.7 32.7 1.0
OP1 B:G12 4.8 27.5 1.0
O3' B:A7 4.8 30.2 1.0
C5' B:U8 4.9 30.6 1.0
O3' B:U8 4.9 30.8 1.0

Magnesium binding site 2 out of 2 in 5omw

Go back to Magnesium Binding Sites List in 5omw
Magnesium binding site 2 out of 2 in the Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mutant T252A of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and Leucyl- Adenylate Analogue in the Aminoacylation Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg101

b:59.5
occ:1.00
OP1 E:U8 2.6 68.1 1.0
OP2 E:G9 2.7 67.4 1.0
P E:G9 3.9 68.4 1.0
OP1 E:U11 4.1 70.5 1.0
OP1 E:G9 4.1 67.1 1.0
P E:U8 4.1 67.6 1.0
O5' E:U8 4.7 68.7 1.0
OP2 E:U11 4.8 71.9 1.0
C5' E:U8 4.9 69.0 1.0
O3' E:U8 4.9 65.7 1.0
O3' E:A7 4.9 69.6 1.0
O5' E:G9 4.9 65.9 1.0
P E:U11 5.0 72.8 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: Mon Sep 30 01:04:00 2024

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