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Sodium in PDB 1ouc: Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V110A Mutant
Enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V110A Mutant
All present enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V110A Mutant:
3.2.1.17;
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 V110A Mutant, PDB code: 1ouc
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 (°) | 56.800, 60.910, 33.830, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 15.3 / 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 V110A Mutant
(pdb code 1ouc). 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 V110A Mutant, PDB code: 1ouc:
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 V110A Mutant, PDB code: 1ouc:
Sodium binding site 1 out of 1 in 1ouc
Go back to
Sodium Binding Sites List in 1ouc
Sodium binding site 1 out
of 1 in the Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V110A Mutant
Mono view
Stereo pair view
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 V110A Mutant within 5.0Å range:
|
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 21:13:31 2024
ISSN: ISSN 0006-2960
PubMed: 9020766
DOI: 10.1021/BI9621829
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