Sandbox Reserved 1131
From Proteopedia
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= Structure = | = Structure = | ||
<Structure load='2ai6' size='350' frame='true' align='right' caption='Solution structure of a Human Phosphohistidine Phosphatase 1 monomer' scene='Insert optional scene name here' /> | <Structure load='2ai6' size='350' frame='true' align='right' caption='Solution structure of a Human Phosphohistidine Phosphatase 1 monomer' scene='Insert optional scene name here' /> | ||
| - | ==Generality== | + | ===Generality=== |
Phosphohistidine phosphatase 1 is a 14kDa homotrimeric protein, which monomers contain all 125 amino acids. | 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. | Furthermore, one monomer contains 4 α helices, 6 β strands and 2 turns. | ||
| - | ==Domains== | + | ===Domains=== |
PHPT1 contains 2 acetylation site and a N-acetylalanine site | PHPT1 contains 2 acetylation site and a N-acetylalanine site | ||
There is also an Janus/Ocnus family region, characteristic. | There is also an Janus/Ocnus family region, characteristic. | ||
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It is located in the cytosol and in extracellular exosome. | It is located in the cytosol and in extracellular exosome. | ||
| - | ==Ligands and binding== | + | ===Ligands and binding=== |
| - | + | There are 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. | O4 S is a 96 Da molecule, with two negative charges. The four oxygens allow good fixation on the monomers, with hydrogen bounds. | ||
Revision as of 21:12, 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
There are 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>
