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

Enzymatic activity of 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;

Protein crystallography data

The structure of Contribution of Hydrophobic Effect to the Conformational Stability of Human Lysozyme, PDB code: 2bqo 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 (°) 56.890, 60.610, 33.220, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / n/a

Sodium Binding Sites:

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

Sodium binding site 1 out of 1 in 2bqo

Go back to Sodium Binding Sites List in 2bqo
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:70.7
occ:1.00
O A:HOH276 3.2 16.3 1.0

Reference:

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
Page generated: Tue Dec 15 05:46:14 2020

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