Sodium in PDB 2meh: 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: 2meh was solved by J.Funahashi, 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 (°)	56.790, 60.970, 33.820, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / n/a

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

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:Na601 b:46.8 occ:1.00 O A:HOH158 2.2 29.5 1.0 O A:HOH138 2.7 16.8 1.0 O A:HOH450 4.8 44.2 1.0 O A:HOH155 4.9 19.5 1.0

J.Funahashi, K.Takano, Y.Yamagata, K.Yutani. Contribution of Amino Acid Substitutions at Two Different Interior Positions to the Conformational Stability of Human Lysozyme Protein Eng. V. 12 841 1999.
ISSN: ISSN 0269-2139
PubMed: 10556244
DOI: 10.1093/PROTEIN/12.10.841