Sandbox Reserved 1491: Difference between revisions

Line 29:

- <scene name='80/802665/Oga/1'>OGA</scene>: two binding sites (chains A and B).

- EDO: three binding sites, only in chain A. They are linked to 2xml by hydrogen bond.

- <scene name='80/802665/Edo/1'>EDO</scene>: three binding sites, only in chain A. They are linked to 2xml by hydrogen bond.

- Zn2+: two binding sites (chains A and B). It makes four coordination bonds : with three cysteines and one histidine.

- <scene name='80/802665/Zn/1'>Zn2+</scene>: two binding sites (chains A and B). It makes four coordination bonds : with three cysteines and one histidine.

- Ni2+ : two binding sites (chains A and B). It makes five coordination bonds : two with OGA, two with two histidine and a last one with a glutamic acid.

- <scene name='80/802665/Ni/1'>Ni2+</scene> : two binding sites (chains A and B). It makes five coordination bonds : two with OGA, two with two histidine and a last one with a glutamic acid.

- Cl- : one binding site, only in chain A.

- <scene name='80/802665/Cl/1'>Cl-</scene> : one binding site, only in chain A.

2xml presents, in each of the two chains, parallel [https://en.wikipedia.org/wiki/Beta_sheet β sheets] around OGA, forming an '''hydrophobic pocket''' (mainly made of aromatic acid). OGA interacts with 2xml amino acids through hydrogen bonds and coordination bonds with Ni2+.

2xml presents, in each of the two chains, parallel [https://en.wikipedia.org/wiki/Beta_sheet β sheets] around <scene name='80/802665/Oga_pocket/1'>OGA</scene>, forming an '''hydrophobic pocket''' (mainly made of aromatic acid). OGA interacts with 2xml amino acids through hydrogen bonds and coordination bonds with Ni2+.

The sequence of the domain has been particularly preserved around OGA (when the protein is folded)<ref>http://consurf.tau.ac.il/fgij/fg.htm?mol=/temp/2XMLA_ConSurf_DB_pipe.pdb </ref>. Thus, the 3D structure has been very preserved as well, indicating that the structure around OGA is essential.

Sandbox Reserved 1491: Difference between revisions

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@@ Line 29: / Line 29: @@
 - <scene name='80/802665/Oga/1'>OGA</scene>: two binding sites (chains A and B).
-- EDO: three binding sites, only in chain A. They are linked to 2xml by hydrogen bond.
+- <scene name='80/802665/Edo/1'>EDO</scene>: three binding sites, only in chain A. They are linked to 2xml by hydrogen bond.
-- Zn2+: two binding sites (chains A and B). It makes four coordination bonds : with three cysteines and one histidine.
+- <scene name='80/802665/Zn/1'>Zn2+</scene>: two binding sites (chains A and B). It makes four coordination bonds : with three cysteines and one histidine.
-- Ni2+ : two binding sites (chains A and B). It makes five coordination bonds : two with OGA, two with two histidine and a last one with a glutamic acid.
+- <scene name='80/802665/Ni/1'>Ni2+</scene> : two binding sites (chains A and B). It makes five coordination bonds : two with OGA, two with two histidine and a last one with a glutamic acid.
-- Cl- : one binding site, only in chain A.
+- <scene name='80/802665/Cl/1'>Cl-</scene> : one binding site, only in chain A.
-xml presents, in each of the two chains, parallel [https://en.wikipedia.org/wiki/Beta_sheet β sheets] around OGA, forming an '''hydrophobic pocket''' (mainly made of aromatic acid). OGA interacts with 2xml amino acids through hydrogen bonds and coordination bonds with Ni2+.
+xml presents, in each of the two chains, parallel [https://en.wikipedia.org/wiki/Beta_sheet β sheets] around <scene name='80/802665/Oga_pocket/1'>OGA</scene>, forming an '''hydrophobic pocket''' (mainly made of aromatic acid). OGA interacts with 2xml amino acids through hydrogen bonds and coordination bonds with Ni2+.
 The sequence of the domain has been particularly preserved around OGA (when the protein is folded)<ref>http://consurf.tau.ac.il/fgij/fg.htm?mol=/temp/2XMLA_ConSurf_DB_pipe.pdb </ref>. Thus, the 3D structure has been very preserved as well, indicating that the structure around OGA is essential.