Sodium in PDB 2bqd: Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme

All present enzymatic activity of Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme:
3.2.1.17;

The structure of Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme, PDB code: 2bqd was solved by K.Takano, Y.Yamagata, K.Yutani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.990, 60.760, 33.470, 90.00, 90.00, 90.00
R / Rfree (%)	17 / n/a

The binding sites of Sodium atom in the Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme (pdb code 2bqd). 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 Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme, PDB code: 2bqd:

Sodium binding site 1 out of 1 in the Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Na131 b:56.3 occ:1.00 O A:HOH233 3.5 17.9 1.0

K.Takano, Y.Yamagata, K.Yutani. A General Rule For the Relationship Between Hydrophobic Effect and Conformational Stability of A Protein: Stability and Structure of A Series of Hydrophobic Mutants of Human Lysozyme. J.Mol.Biol. V. 280 749 1998.
ISSN: ISSN 0022-2836
PubMed: 9677301
DOI: 10.1006/JMBI.1998.1906