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Sodium in PDB 4g6z: Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate

Enzymatic activity of Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate

All present enzymatic activity of Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate:
6.1.1.17;

Protein crystallography data

The structure of Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate, PDB code: 4g6z was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.62 / 2.05
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 88.950, 88.950, 132.270, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 23.7

Other elements in 4g6z:

The structure of Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate (pdb code 4g6z). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate, PDB code: 4g6z:

Sodium binding site 1 out of 1 in 4g6z

Go back to Sodium Binding Sites List in 4g6z
Sodium binding site 1 out of 1 in the Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of A Glutamyl-Trna Synthetase Glurs From Burkholderia Thailandensis Bound to L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na503

b:72.5
occ:1.00
 O A:HOH788 2.3 47.9 1.0
O A:HOH787 2.5 62.0 1.0
O A:GLY346 2.7 51.6 1.0
O A:GLU344 2.7 60.1 1.0
O A:ILE343 3.0 60.9 1.0
O A:PRO347 3.2 49.3 1.0
C A:GLU344 3.4 63.2 1.0
C A:PRO347 3.6 48.8 1.0
C A:GLY346 3.7 53.6 1.0
CA A:GLU344 3.7 64.3 1.0
CA A:ASP348 3.9 51.4 1.0
N A:ASP348 3.9 49.1 1.0
C A:ILE343 4.0 60.3 1.0
N A:GLY346 4.3 59.6 1.0
N A:GLU344 4.4 62.7 1.0
N A:GLN345 4.4 64.9 1.0
N A:PRO347 4.6 49.4 1.0
CA A:PRO347 4.6 49.7 1.0
C A:GLN345 4.6 64.8 1.0
CA A:GLY346 4.6 56.0 1.0
N A:LEU349 4.7 48.0 1.0
C A:ASP348 4.8 48.3 1.0
CB A:ASP348 4.8 54.5 1.0
CA A:GLN345 5.0 65.8 1.0

Reference:

S.O.Moen, T.E.Edwards, D.M.Dranow, M.C.Clifton, B.Sankaran, W.C.Van Voorhis, A.Sharma, C.Manoil, B.L.Staker, P.J.Myler, D.D.Lorimer. Ligand Co-Crystallization of Aminoacyl-Trna Synthetases From Infectious Disease Organisms. Sci Rep V. 7 223 2017.
ISSN: ESSN 2045-2322
PubMed: 28303005
DOI: 10.1038/S41598-017-00367-6
Page generated: Mon Oct 7 15:31:23 2024

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