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Sodium in PDB 2hec: 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;

Protein crystallography data

The structure of Contribution of Water Molecules in the Interior of A Protein to the Conformational Stability, PDB code: 2hec 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 (°) 56.730, 61.040, 33.800, 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 Water Molecules in the Interior of A Protein to the Conformational Stability (pdb code 2hec). 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: 2hec:

Sodium binding site 1 out of 1 in 2hec

Go back to Sodium Binding Sites List in 2hec
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

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:
probe atom residue distance (Å) B Occ
A:Na601

b:37.8
occ:1.00
O A:HOH162 2.2 34.9 1.0
O A:HOH141 2.6 13.8 1.0
O A:HOH260 4.8 39.1 1.0
O A:HOH147 4.8 19.7 1.0

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 02:46:29 2024

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