3u3k: Difference between revisions

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New page: '''Unreleased structure''' The entry 3u3k is ON HOLD until Paper Publication Authors: Guttman, C., Berger, I., Aharoni, A., Zarivach, R. Description: Crystal structure of hSULT1A1 boun...
 
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'''Unreleased structure'''


The entry 3u3k is ON HOLD  until Paper Publication
==Crystal structure of hSULT1A1 bound to PAP and 2-Naphtol==
<StructureSection load='3u3k' size='340' side='right'caption='[[3u3k]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3u3k]] is a 2 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=3U3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3K FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=03V:NAPHTHALEN-2-OL'>03V</scene>, <scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></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=3u3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3k OCA], [https://pdbe.org/3u3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3k RCSB], [https://www.ebi.ac.uk/pdbsum/3u3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ST1A1_HUMAN ST1A1_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.<ref>PMID:12471039</ref> <ref>PMID:16221673</ref>


Authors: Guttman, C., Berger, I., Aharoni, A., Zarivach, R.
==See Also==
 
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
Description: Crystal structure of hSULT1A1 bound to PAP and 2-Naphtol
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aharoni A]]
[[Category: Berger I]]
[[Category: Guttman C]]
[[Category: Zarivach R]]

Latest revision as of 16:47, 14 March 2024

Crystal structure of hSULT1A1 bound to PAP and 2-NaphtolCrystal structure of hSULT1A1 bound to PAP and 2-Naphtol

Structural highlights

3u3k is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.36Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ST1A1_HUMAN Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.[1] [2]

See Also

References

  1. ↑ Gamage NU, Duggleby RG, Barnett AC, Tresillian M, Latham CF, Liyou NE, McManus ME, Martin JL. Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem. 2003 Feb 28;278(9):7655-62. Epub 2002 Dec 5. PMID:12471039 doi:http://dx.doi.org/10.1074/jbc.M207246200
  2. ↑ Gamage NU, Tsvetanov S, Duggleby RG, McManus ME, Martin JL. The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem. 2005 Dec 16;280(50):41482-6. Epub 2005 Oct 12. PMID:16221673 doi:10.1074/jbc.M508289200

3u3k, resolution 2.36Å

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