Sodium in PDB 6ti3: Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine

All present enzymatic activity of Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine:
2.1.2.1;

The structure of Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine, PDB code: 6ti3 was solved by G.Petrillo, K.Hernandez, J.Bujons, P.Clapes, I.Uson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.09 / 1.96
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	200.393, 113.692, 133.147, 90.00, 94.51, 90.00
R / Rfree (%)	18.1 / n/a

The binding sites of Sodium atom in the Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine (pdb code 6ti3). 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 Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine, PDB code: 6ti3:

Sodium binding site 1 out of 1 in the Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Apo-Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with D-Threonine within 5.0Å range: probe atom residue distance (Å) B Occ D:Na501 b:65.0 occ:1.00 O D:ALA203 2.5 40.4 1.0 O D:HIS229 2.8 54.1 1.0 N D:LEU232 3.2 40.9 1.0 N D:THR231 3.3 42.6 1.0 OG1 D:THR231 3.6 50.2 1.0 CB D:LYS230 3.6 44.5 1.0 CB D:ALA206 3.6 44.8 1.0 C D:ALA203 3.7 38.9 1.0 CB D:LEU232 3.7 42.0 1.0 C D:LYS230 3.8 43.2 1.0 O D:THR227 3.8 46.8 1.0 C D:HIS229 3.8 48.6 1.0 CA D:LYS230 4.0 45.2 1.0 CA D:THR231 4.0 44.6 1.0 N D:ALA206 4.0 41.4 1.0 OG1 D:THR227 4.0 44.1 1.0 C D:THR231 4.1 44.8 1.0 CA D:LEU232 4.1 39.4 1.0 OG1 D:THR226 4.1 40.0 1.0 N D:GLY207 4.2 40.6 1.0 CA D:ALA206 4.3 43.3 1.0 N D:LYS230 4.3 44.4 1.0 CA D:ALA203 4.3 42.6 1.0 CB D:THR231 4.4 45.0 1.0 O D:HIS204 4.6 50.2 1.0 CG D:LYS230 4.6 45.1 1.0 C D:THR227 4.6 41.3 1.0 O D:LYS230 4.6 39.8 1.0 C D:ALA206 4.6 41.4 1.0 C D:HIS204 4.7 50.9 1.0 N D:HIS204 4.7 36.0 1.0 O D:MET202 4.8 44.3 1.0 N D:HIS229 4.9 40.7 1.0 CD D:LYS230 4.9 44.5 1.0 CA D:HIS204 4.9 46.4 1.0 C D:THR228 4.9 42.3 1.0

G.Petrillo, K.Hernandez, J.Bujons, P.Clapes, I.Uson. Structural Insights Into Nucleophile Substrate Specificity in Variants of N-Serine Hydroxymethyltransferase From Streptococcus Thermophilus To Be Published.