Sodium in PDB 2deh: Crystal Structure of TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions

The structure of Crystal Structure of TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions, PDB code: 2deh was solved by E.Inagaki, N.Nakano, A.Shinkai, S.Yokoyama, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.98 / 2.45
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	65.171, 65.171, 202.364, 90.00, 90.00, 90.00
R / Rfree (%)	24.3 / 27.9

The structure of Crystal Structure of TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions (pdb code 2deh). 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 TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions, PDB code: 2deh:

Sodium binding site 1 out of 1 in the Crystal Structure of TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions


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 TT0972 Protein Form Thermus Thermophilus with Cl(-) Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1001 b:74.5 occ:1.00 OE1 C:GLU19 2.3 60.3 1.0 OE2 A:GLU19 2.5 57.0 1.0 OE1 A:GLU19 2.6 58.7 1.0 OE2 C:GLU19 2.9 62.3 1.0 CD A:GLU19 2.9 58.5 1.0 CD C:GLU19 2.9 61.4 1.0 OE1 B:GLU19 3.1 68.7 1.0 OE2 B:GLU19 3.2 67.6 1.0 CD B:GLU19 3.6 68.9 1.0 CG C:GLU19 4.4 57.3 1.0 CG A:GLU19 4.4 60.1 1.0 CB C:LEU18 4.5 56.0 1.0 N C:LEU18 4.6 62.0 1.0 N C:GLU19 4.6 55.8 1.0 CG C:LEU18 4.9 54.2 1.0 CD1 C:LEU18 4.9 53.3 1.0 CB C:GLU19 5.0 56.0 1.0

E.Inagaki, N.Nakano, A.Shinkai, S.Yokoyama. Crystal Structure of TT0972 Protein Form Thermus Thermophilus To Be Published.