Calcium in PDB 4pqi: Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa

The structure of Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa, PDB code: 4pqi 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)	38.51 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.524, 77.013, 82.636, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 22.3

The binding sites of Calcium atom in the Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa (pdb code 4pqi). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa, PDB code: 4pqi:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca302 b:54.0 occ:1.00 O A:HOH432 2.3 53.5 1.0 O A:HOH416 2.4 39.4 1.0 O A:PHE164 2.4 46.6 1.0 O A:HOH470 2.5 43.4 1.0 O A:GLY167 2.5 47.7 1.0 O A:HOH414 2.5 39.9 1.0 O A:LEU161 3.0 43.6 1.0 C A:PHE164 3.6 47.4 1.0 C A:GLY167 3.7 47.5 1.0 CA A:ASP165 4.0 50.8 1.0 C A:LEU161 4.2 43.6 1.0 OD1 A:ASP165 4.2 46.8 1.0 N A:ASP165 4.3 47.9 1.0 N A:GLY167 4.4 43.4 1.0 NZ A:LYS207 4.4 64.1 1.0 CA A:PRO168 4.4 47.3 1.0 N A:PRO168 4.5 47.7 1.0 O A:HOH438 4.6 57.0 1.0 C A:ASP165 4.6 51.9 1.0 CA A:GLY167 4.6 40.9 1.0 O A:PHE169 4.7 42.2 1.0 O A:HOH407 4.7 36.2 1.0 CA A:PHE164 4.8 43.2 1.0 N A:ASP166 4.8 50.6 1.0 O A:HOH495 4.8 58.5 1.0 C A:PRO168 4.8 43.2 1.0 N A:PHE164 4.8 39.1 1.0 CE A:LYS207 4.9 60.1 1.0 O A:HOH440 4.9 44.3 1.0 CD A:LYS207 5.0 55.5 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca303 b:42.4 occ:1.00 O A:HOH427 2.2 41.8 1.0 O A:HIS162 2.4 40.3 1.0 O A:HOH471 2.4 45.2 1.0 OD2 A:ASP165 2.4 47.2 1.0 O A:HOH410 2.5 42.6 1.0 OD1 A:ASP165 2.6 46.8 1.0 CG A:ASP165 2.8 46.1 1.0 C A:HIS162 3.5 41.8 1.0 CA A:HIS162 4.1 41.1 1.0 CB A:HIS162 4.2 42.5 1.0 O A:HOH416 4.3 39.4 1.0 CB A:ASP165 4.3 48.1 1.0 O A:LYS163 4.4 39.0 1.0 ND1 A:HIS162 4.6 45.2 1.0 N A:LYS163 4.6 42.7 1.0 O A:HOH495 4.6 58.5 1.0 C A:LYS163 4.6 40.6 1.0 CA A:LYS163 4.8 45.2 1.0 CG A:HIS162 4.9 44.2 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Glutathione Transferase LAMBDA3 From Populus Trichocarpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca304 b:50.0 occ:1.00 O A:HOH406 2.3 45.9 1.0 O A:GLY55 2.4 44.1 1.0 OE2 A:GLU59 2.4 58.6 1.0 O A:HOH425 2.5 50.0 1.0 O A:HOH431 2.5 57.2 1.0 OE1 A:GLU59 2.5 47.7 1.0 O A:HOH496 2.7 49.5 1.0 CD A:GLU59 2.8 54.1 1.0 C A:GLY55 3.6 43.5 1.0 CA A:LEU56 4.2 45.2 1.0 CG A:GLU59 4.3 52.8 1.0 N A:LEU56 4.4 43.2 1.0 O A:HOH514 4.5 47.6 1.0 O A:HOH433 4.6 53.8 1.0 O A:HOH509 4.6 58.8 1.0 CA A:GLY55 4.7 42.3 1.0 C A:LEU56 4.7 45.9 1.0 N A:GLN57 4.7 48.4 1.0 N A:ASP58 4.8 52.0 1.0 CB A:ASP58 4.8 64.6 1.0 N A:GLU59 4.9 44.8 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