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Sodium in PDB 6ti1: Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex

Enzymatic activity of Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex

All present enzymatic activity of Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex:
2.1.2.1;

Protein crystallography data

The structure of Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex, PDB code: 6ti1 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) 98.48 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 114.708, 114.708, 192.063, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex (pdb code 6ti1). 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 Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex, PDB code: 6ti1:

Sodium binding site 1 out of 1 in 6ti1

Go back to Sodium Binding Sites List in 6ti1
Sodium binding site 1 out of 1 in the Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Shmt From Streptococcus Thermophilus TYR55SER Variant in Complex with Plp/L-Threonine/LYS230 Gem Diamine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na503

b:48.6
occ:1.00
 O A:HIS229 2.7 35.4 1.0
O A:ALA203 2.7 35.2 1.0
N A:LEU232 3.0 39.0 1.0
N A:THR231 3.2 34.9 1.0
CB A:LEU232 3.3 36.4 1.0
OG1 A:THR231 3.5 36.4 1.0
CB A:LYS230 3.6 34.4 1.0
CB A:ALA206 3.6 34.0 1.0
C A:HIS229 3.6 37.8 1.0
C A:LYS230 3.6 32.4 1.0
O A:THR227 3.8 32.9 1.0
CA A:LEU232 3.8 36.8 1.0
CA A:LYS230 3.9 33.9 1.0
C A:THR231 3.9 39.1 1.0
C A:ALA203 3.9 37.2 1.0
OG1 A:THR227 4.0 34.5 1.0
CA A:THR231 4.0 38.8 1.0
N A:ALA206 4.1 36.0 1.0
N A:LYS230 4.1 33.3 1.0
N A:GLY207 4.1 33.1 1.0
OG1 A:THR226 4.2 36.1 1.0
CA A:ALA206 4.3 35.0 1.0
CB A:THR231 4.4 39.9 1.0
O A:LYS230 4.5 38.4 1.0
CG A:LYS230 4.6 39.0 1.0
C A:ALA206 4.6 34.6 1.0
CA A:ALA203 4.6 33.6 1.0
C A:THR227 4.7 37.3 1.0
O A:HIS204 4.7 35.5 1.0
O A:THR228 4.7 33.0 1.0
CG A:LEU232 4.7 34.8 1.0
C A:HIS204 4.8 38.0 1.0
C A:THR228 4.8 37.0 1.0
CA A:HIS229 4.8 37.1 1.0
N A:HIS229 4.9 35.0 1.0
C A:LEU232 4.9 34.2 1.0
CD2 A:LEU232 4.9 41.0 1.0
N A:ARG233 4.9 32.6 1.0
N A:HIS204 5.0 35.7 1.0

Reference:

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.
Page generated: Tue Oct 8 13:58:03 2024

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