Sodium »
PDB 2gum-2hti »
2hef »
Sodium in PDB 2hef: Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability
Enzymatic activity of Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability
All present enzymatic activity of Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability:
3.2.1.17;
3.2.1.17;
Protein crystallography data
The structure of Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability, PDB code: 2hef
was solved by
K.Takano,
J.Funahashi,
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 (°) | 56.750, 60.970, 33.740, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 16 / n/a |
Sodium Binding Sites:
The binding sites of Sodium atom in the Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability
(pdb code 2hef). 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 Water Molecules in the Interior of A Protein to the Conformational Stability, PDB code: 2hef:
In total only one binding site of Sodium was determined in the Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability, PDB code: 2hef:
Sodium binding site 1 out of 1 in 2hef
Go back to
Sodium Binding Sites List in 2hef
Sodium binding site 1 out
of 1 in the Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability
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 Water Molecules in the Interior of A Protein to the Conformational Stability within 5.0Å range:
|
Reference:
K.Takano,
J.Funahashi,
Y.Yamagata,
S.Fujii,
K.Yutani.
Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability. J.Mol.Biol. V. 274 132 1997.
ISSN: ISSN 0022-2836
PubMed: 9398521
DOI: 10.1006/JMBI.1997.1365
Page generated: Mon Oct 7 02:46:38 2024
ISSN: ISSN 0022-2836
PubMed: 9398521
DOI: 10.1006/JMBI.1997.1365
Last articles
Zn in 9MJ5Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
