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Sodium in PDB 1b5x: Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants

Enzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants

All present enzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants:
3.2.1.17;

Protein crystallography data

The structure of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants, PDB code: 1b5x was solved by K.Takano, Y.Yamagata, M.Kubota, J.Funahashi, 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 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.360, 62.620, 32.550, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants (pdb code 1b5x). 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 Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants, PDB code: 1b5x:

Sodium binding site 1 out of 1 in 1b5x

Go back to Sodium Binding Sites List in 1b5x
Sodium binding site 1 out of 1 in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutants within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na601

b:9.2
occ:1.00
O A:HOH154 2.3 8.8 1.0
O A:HOH152 2.4 4.9 1.0
O A:HOH153 4.4 7.3 1.0

Reference:

K.Takano, Y.Yamagata, M.Kubota, J.Funahashi, S.Fujii, K.Yutani. Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser --> Ala Mutants. Biochemistry V. 38 6623 1999.
ISSN: ISSN 0006-2960
PubMed: 10350481
DOI: 10.1021/BI9901228
Page generated: Thu Oct 29 03:45:13 2020

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