Sodium in PDB 3vey: Glucokinase in Complex with Glucose and Atpgs

All present enzymatic activity of Glucokinase in Complex with Glucose and Atpgs:
2.7.1.2;

The structure of Glucokinase in Complex with Glucose and Atpgs, PDB code: 3vey was solved by S.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.03 / 2.25
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	80.387, 80.387, 324.334, 90.00, 90.00, 120.00
R / Rfree (%)	21.4 / 24.6

The binding sites of Sodium atom in the Glucokinase in Complex with Glucose and Atpgs (pdb code 3vey). 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 Glucokinase in Complex with Glucose and Atpgs, PDB code: 3vey:

Sodium binding site 1 out of 1 in the Glucokinase in Complex with Glucose and Atpgs


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Glucokinase in Complex with Glucose and Atpgs within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:62.0 occ:1.00 O A:GLY246 2.5 69.7 1.0 O A:MET238 2.7 62.2 1.0 O A:VAL244 2.9 69.8 1.0 O A:VAL241 2.9 61.3 1.0 C A:GLY246 3.6 71.9 1.0 C A:MET238 3.7 61.8 1.0 C A:VAL241 3.8 59.8 1.0 N A:GLY246 3.8 68.9 1.0 C A:VAL244 3.9 69.6 1.0 OD2 A:ASP247 4.1 85.2 1.0 CA A:GLN239 4.1 59.5 1.0 C A:GLU245 4.2 72.0 1.0 N A:GLN239 4.3 59.0 1.0 CA A:GLY246 4.3 68.9 1.0 CA A:GLU245 4.4 68.9 1.0 C A:GLN239 4.4 60.6 1.0 CA A:GLU242 4.4 58.4 1.0 N A:GLU242 4.5 57.1 1.0 O A:GLN239 4.5 61.7 1.0 N A:GLU245 4.6 67.9 1.0 N A:VAL241 4.7 53.1 1.0 N A:ASP247 4.7 70.4 1.0 CA A:VAL241 4.7 52.7 1.0 CA A:MET238 4.8 56.5 1.0 C A:GLU242 4.9 62.4 1.0 O A:GLU245 4.9 70.9 1.0 CB A:MET238 4.9 61.0 1.0 CA A:VAL244 4.9 64.0 1.0 CE A:MET238 5.0 68.1 1.0 N A:VAL244 5.0 62.8 1.0

S.Liu, M.J.Ammirati, X.Song, J.D.Knafels, J.Zhang, S.E.Greasley, J.A.Pfefferkorn, X.Qiu. Insights Into Mechanism of Glucokinase Activation: Observation of Multiple Distinct Protein Conformations. J.Biol.Chem. V. 287 13598 2012.
ISSN: ISSN 0021-9258
PubMed: 22298776
DOI: 10.1074/JBC.M111.274126