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Magnesium in PDB 4as1: Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation

Enzymatic activity of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation

All present enzymatic activity of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation:
6.1.1.4;

Protein crystallography data

The structure of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation, PDB code: 4as1 was solved by A.Palencia, T.Crepin, M.T.Vu, T.L.Lincecum Jr, S.A.Martinis, S.Cusack, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.85 / 2.02
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 89.680, 77.110, 91.140, 90.00, 102.24, 90.00
R / Rfree (%) 20.8 / 24.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation (pdb code 4as1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation, PDB code: 4as1:

Magnesium binding site 1 out of 1 in 4as1

Go back to Magnesium Binding Sites List in 4as1
Magnesium binding site 1 out of 1 in the Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole AN2679 in the Editing Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1076

b:50.1
occ:1.00
 O B:HOH2004 2.1 43.8 1.0
OP1 B:U8 2.2 43.1 1.0
OP2 B:G9 2.3 43.8 1.0
O B:HOH2003 2.4 42.3 1.0
P B:U8 3.4 45.2 1.0
O B:HOH2006 3.4 37.6 1.0
P B:G9 3.7 43.9 1.0
OP2 B:U8 3.8 43.8 1.0
O5' B:U8 4.0 42.1 1.0
OP1 B:U11 4.2 48.2 1.0
O B:HOH2010 4.4 36.9 1.0
O5' B:G9 4.4 41.0 1.0
C3' B:U8 4.5 40.5 1.0
OP2 B:G12 4.5 45.6 1.0
O3' B:U8 4.6 43.3 1.0
C5' B:G9 4.6 39.8 1.0
C5' B:U8 4.7 43.7 1.0
O3' B:A7 4.7 47.1 1.0
OP1 B:G9 4.7 48.0 1.0

Reference:

A.Palencia, T.Crepin, M.T.Vu, T.L.Lincecum Jr, S.A.Martinis, S.Cusack. Structural Dynamics of the Aminoacylation and Proofreading Functional Cycle of Bacterial Leucyl-Trna Synthetase Nat.Struct.Mol.Biol. V. 19 677 2012.
ISSN: ISSN 1545-9993
PubMed: 22683997
DOI: 10.1038/NSMB.2317
Page generated: Thu Aug 15 14:41:19 2024

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