Atomistry » Sodium » PDB 131d-1b7r » 1b5u
Atomistry »
  Sodium »
    PDB 131d-1b7r »
      1b5u »

Sodium in PDB 1b5u: Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant

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

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 Mutant:
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 Mutant, PDB code: 1b5u 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 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.960, 60.980, 33.780, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 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 Mutant (pdb code 1b5u). 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 Mutant, PDB code: 1b5u:

Sodium binding site 1 out of 1 in 1b5u

Go back to Sodium Binding Sites List in 1b5u
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 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 Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na331

b:34.6
occ:1.00
O A:HOH158 2.2 32.6 1.0
O A:HOH145 2.4 12.6 1.0
O A:HOH144 4.7 17.5 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: Sun Oct 6 17:53:04 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy