Sodium in PDB 1hzc: Bacillus Caldolyticus Cold-Shock Protein Mutants to Study Determinants of Protein Stability

The structure of Bacillus Caldolyticus Cold-Shock Protein Mutants to Study Determinants of Protein Stability, PDB code: 1hzc was solved by H.Delbrueck, U.Mueller, D.Perl, F.X.Schmid, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.32
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	76.864, 76.864, 48.024, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 18.1

The binding sites of Sodium atom in the Bacillus Caldolyticus Cold-Shock Protein Mutants to Study Determinants of Protein Stability (pdb code 1hzc). 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 Bacillus Caldolyticus Cold-Shock Protein Mutants to Study Determinants of Protein Stability, PDB code: 1hzc:

Sodium binding site 1 out of 1 in the Bacillus Caldolyticus Cold-Shock Protein Mutants to Study Determinants of Protein Stability


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Bacillus Caldolyticus Cold-Shock Protein Mutants to Study Determinants of Protein Stability within 5.0Å range: probe atom residue distance (Å) B Occ A:Na305 b:19.7 occ:1.00 O A:HOH316 2.5 15.6 1.0 O A:VAL20 2.5 14.9 1.0 O A:HOH400 2.7 33.1 1.0 O A:GLY23 2.8 15.7 1.0 O A:HOH426 2.8 44.0 0.5 O A:HOH390 2.9 40.2 0.5 C A:VAL20 3.6 14.1 1.0 C A:GLY23 3.9 14.0 1.0 N A:GLY23 3.9 14.9 1.0 N A:VAL20 4.1 14.1 1.0 N A:GLY22 4.1 15.4 1.0 O A:HOH421 4.4 26.0 0.5 CA A:VAL20 4.4 14.0 1.0 CA A:GLU21 4.5 14.6 1.0 N A:GLU21 4.5 14.3 1.0 CA A:GLY23 4.6 14.8 1.0 OD1 A:ASP25 4.6 16.8 1.0 C A:GLU21 4.7 14.3 1.0 C A:GLY22 4.8 15.8 1.0 CB A:GLU19 4.9 17.5 1.0 CA A:GLY22 4.9 16.1 1.0 N A:SER24 5.0 13.5 1.0

H.Delbruck, U.Mueller, D.Perl, F.X.Schmid, U.Heinemann. Crystal Structures of Mutant Forms of the Bacillus Caldolyticus Cold Shock Protein Differing in Thermal Stability. J.Mol.Biol. V. 313 359 2001.
ISSN: ISSN 0022-2836
PubMed: 11800562
DOI: 10.1006/JMBI.2001.5051