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8agf

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Current revision (13:37, 1 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8agf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AGF FirstGlance]. <br>
<table><tr><td colspan='2'>[[8agf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AGF FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8agf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8agf OCA], [https://pdbe.org/8agf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8agf RCSB], [https://www.ebi.ac.uk/pdbsum/8agf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8agf ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8agf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8agf OCA], [https://pdbe.org/8agf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8agf RCSB], [https://www.ebi.ac.uk/pdbsum/8agf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8agf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/THTR_HUMAN THTR_HUMAN]] Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA.<ref>PMID:20663881</ref> <ref>PMID:21685364</ref>
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[https://www.uniprot.org/uniprot/THTR_HUMAN THTR_HUMAN] Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA.<ref>PMID:20663881</ref> <ref>PMID:21685364</ref>
== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of human Thiosulfate sulfurtransferase amino acids 2-297

PDB ID 8agf

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