Sandbox Reserved 1131
From Proteopedia
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It has one substrate binding site, and one proton acceptor active site. | It has one substrate binding site, and one proton acceptor active site. | ||
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| + | =Function= | ||
| + | It is an hydrolase. | ||
| + | This characteristic structure allows it to have many activities : phosphoprotein and phosphohistidine phosphatase, calcium channel inhibition, ion channel binding. | ||
| + | It is located in the cytosol and in extracellular exosome. | ||
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| + | ==Ligands and binding== | ||
| + | Hypothèse : There is 6 SO4 lingands, called SO4 201 to 206. 2 lingand fix to each monomer (2ai6), inducing a conformational change of all the monomers (2hw4). Then, the fix lingands bind to each other, forming a trimer (2NMM). | ||
| + | O4 S is a 96 Da molecule, with two negative charges. The four oxygens allow good fixation on the monomers, with hydrogen bounds. | ||
| + | |||
= Disease = | = Disease = | ||
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= Structural highlights = | = Structural highlights = | ||
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| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:10, 28 January 2016
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| This Sandbox is Reserved from 15/12/2015, through 15/06/2016 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1120 through Sandbox Reserved 1159. |
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(Human) Phosphohistidine phosphatase 1 belongs to the Janus family, and has 2 isoforms produced by alternative splicing, and 6 transcripts. It is encoded by the PHPT1 gene, located on the 9th chromosome.
Contents |
Structure
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Generality
Phosphohistidine phosphatase 1 is a 14kDa homotrimeric protein, which monomers contain all 125 amino acids. Furthermore, one monomer contains 4 α helices, 6 β strands and 2 turns.
Domains
PHPT1 contains 2 acetylation site and a N-acetylalanine site There is also an Janus/Ocnus family region, characteristic.
It has one substrate binding site, and one proton acceptor active site.
Function
It is an hydrolase. This characteristic structure allows it to have many activities : phosphoprotein and phosphohistidine phosphatase, calcium channel inhibition, ion channel binding. It is located in the cytosol and in extracellular exosome.
Ligands and binding
Hypothèse : There is 6 SO4 lingands, called SO4 201 to 206. 2 lingand fix to each monomer (2ai6), inducing a conformational change of all the monomers (2hw4). Then, the fix lingands bind to each other, forming a trimer (2NMM). O4 S is a 96 Da molecule, with two negative charges. The four oxygens allow good fixation on the monomers, with hydrogen bounds.
Disease
Relevance
Structural highlights
</StructureSection>
