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Sodium in PDB 1oue: Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant

Enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant

All present enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant:
3.2.1.17;

Protein crystallography data

The structure of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant, PDB code: 1oue was solved by K.Takano, Y.Yamagata, S.Fujii, 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 (°) 56.700, 61.120, 33.760, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant (pdb code 1oue). 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 Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant, PDB code: 1oue:

Sodium binding site 1 out of 1 in 1oue

Go back to Sodium Binding Sites List in 1oue
Sodium binding site 1 out of 1 in the Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant


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 Residues to the Stability of Human Lysozyme: X-Ray Structure of the V125A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:24.6
occ:1.00
O A:HOH138 2.3 22.6 1.0
O A:HOH149 2.4 13.6 1.0
O A:HOH139 4.4 17.1 1.0
O A:HOH209 4.9 39.0 1.0

Reference:

K.Takano, Y.Yamagata, S.Fujii, K.Yutani. Contribution of the Hydrophobic Effect to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analyses of the Nine Valine to Alanine Mutants. Biochemistry V. 36 688 1997.
ISSN: ISSN 0006-2960
PubMed: 9020766
DOI: 10.1021/BI9621829
Page generated: Sun Oct 6 21:13:39 2024

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