Sodium in PDB 2zk9: Crystal Structure of Protein-Glutaminase

The structure of Crystal Structure of Protein-Glutaminase, PDB code: 2zk9 was solved by R.Hashizume, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.15
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	62.306, 62.306, 185.532, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / 13.6

The binding sites of Sodium atom in the Crystal Structure of Protein-Glutaminase (pdb code 2zk9). 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 Protein-Glutaminase, PDB code: 2zk9:

Sodium binding site 1 out of 1 in the Crystal Structure of Protein-Glutaminase


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 Protein-Glutaminase within 5.0Å range: probe atom residue distance (Å) B Occ X:Na501 b:61.4 occ:1.00 SG X:CYS42 2.2 17.1 1.0 O X:HOH619 2.5 22.6 1.0 CB X:CYS42 2.8 11.7 1.0 N X:CYS42 2.9 9.2 1.0 O X:HOH789 2.9 40.5 1.0 O X:HOH565 3.0 22.4 0.5 O X:HOH565 3.3 8.5 0.5 CA X:CYS42 3.4 9.3 1.0 N X:GLY41 3.6 9.5 1.0 OD2 X:ASP40 3.7 14.3 0.7 CA X:ASP40 3.8 9.2 0.7 C X:ASP40 3.8 8.5 0.7 C X:GLY41 4.0 8.4 1.0 C X:ASP40 4.0 10.3 0.3 CA X:ASP40 4.1 11.6 0.3 O X:HOH759 4.2 47.2 1.0 CA X:GLY41 4.3 9.4 1.0 OD1 X:ASP40 4.3 21.2 0.3 N X:TYR43 4.5 8.4 1.0 C X:CYS42 4.5 8.2 1.0 CG X:ASP40 4.5 12.5 0.7 O X:ASP40 4.6 8.7 0.7 ND1 X:HIS83 4.7 10.7 1.0 CD1 X:TYR43 4.7 11.1 1.0 O X:HOH806 4.7 60.9 1.0 O X:TYR82 4.7 9.7 1.0 CB X:ASP40 4.7 10.8 0.7 N X:ASP40 4.7 9.3 0.7 OH X:TYR82 4.7 24.0 1.0 NE1 X:TRP80 4.7 11.3 1.0 N X:ASP40 4.8 10.7 0.3 CZ X:TYR82 4.8 19.7 1.0 O X:VAL39 4.9 12.3 1.0 O X:ASP40 4.9 9.6 0.3 CD1 X:TRP80 4.9 11.5 1.0 CE1 X:TYR43 5.0 12.0 1.0

R.Hashizume, Y.Maki, K.Mizutani, N.Takahashi, H.Matsubara, A.Sugita, K.Sato, S.Yamaguchi, B.Mikami. Crystal Structures of Protein Glutaminase and Its Pro Forms Converted Into Enzyme-Substrate Complex J.Biol.Chem. V. 286 38691 2011.
ISSN: ISSN 0021-9258
PubMed: 21926168
DOI: 10.1074/JBC.M111.255133