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Sodium in PDB 1ouj: Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V99A Mutant

Enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V99A Mutant

All present enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V99A 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 V99A Mutant, PDB code: 1ouj 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 (°) 56.730, 61.090, 33.920, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 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 V99A Mutant (pdb code 1ouj). 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 V99A Mutant, PDB code: 1ouj:

Sodium binding site 1 out of 1 in 1ouj

Go back to Sodium Binding Sites List in 1ouj
Sodium binding site 1 out of 1 in the Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the V99A 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 V99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:22.5
occ:1.00
O A:HOH395 2.3 26.1 1.0
O A:HOH141 2.4 13.6 1.0
O A:HOH138 4.6 15.7 1.0
O A:HOH264 5.0 30.2 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 21:13:51 2024

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