Sodium in PDB 4pqh: Crystal Structure of Glutathione Transferase LAMBDA1 From Populus Trichocarpa

The structure of Crystal Structure of Glutathione Transferase LAMBDA1 From Populus Trichocarpa, PDB code: 4pqh was solved by P.A.Lallement, E.Meux, J.M.Gualberto, P.Prosper, C.Didierjean, A.Haouz, F.Saul, N.Rouhier, A.Hecker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.50 / 1.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	33.009, 45.835, 66.739, 91.53, 102.43, 96.26
R / Rfree (%)	14.8 / 19.3

The binding sites of Sodium atom in the Crystal Structure of Glutathione Transferase LAMBDA1 From Populus Trichocarpa (pdb code 4pqh). 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 Glutathione Transferase LAMBDA1 From Populus Trichocarpa, PDB code: 4pqh:

Sodium binding site 1 out of 1 in the Crystal Structure of Glutathione Transferase LAMBDA1 From Populus Trichocarpa


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 Glutathione Transferase LAMBDA1 From Populus Trichocarpa within 5.0Å range: probe atom residue distance (Å) B Occ B:Na301 b:28.8 occ:1.00 OE2 B:GLU207 2.7 14.6 1.0 CD B:GLU207 3.5 13.1 1.0 CG B:GLU207 3.6 13.3 1.0 CB B:ALA203 3.6 12.6 1.0 O B:ALA203 3.7 12.3 1.0 CA B:ALA203 3.9 11.5 1.0 C B:ALA203 4.1 10.2 1.0 CB B:GLU206 4.3 16.2 1.0 O B:HOH480 4.4 29.9 1.0 OE1 B:GLU207 4.7 13.8 1.0 NZ B:LYS210 4.7 15.9 1.0 N B:GLU207 4.8 10.8 1.0 O B:HOH657 4.8 31.6 1.0 CB B:GLU207 4.9 11.1 1.0

P.A.Lallement, E.Meux, J.M.Gualberto, P.Prosper, C.Didierjean, F.Saul, A.Haouz, N.Rouhier, A.Hecker. Structural and Enzymatic Insights Into Lambda Glutathione Transferases From Populus Trichocarpa, Monomeric Enzymes Constituting An Early Divergent Class Specific to Terrestrial Plants. Biochem.J. V. 462 39 2014.
ISSN: ISSN 0264-6021
PubMed: 24825169
DOI: 10.1042/BJ20140390