3qvv: Difference between revisions

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'''Unreleased structure'''


The entry 3qvv is ON HOLD
==Crystal structure of Ancestral variant b9 of SULT 1A1 in complex with PAP and 3-CyC==
<StructureSection load='3qvv' size='340' side='right'caption='[[3qvv]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qvv]] 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=3QVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QVV 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3QV:7-HYDROXY-2-OXO-2H-CHROMENE-3-CARBONITRILE'>3QV</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=3qvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qvv OCA], [https://pdbe.org/3qvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qvv RCSB], [https://www.ebi.ac.uk/pdbsum/3qvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qvv 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: Alcolombri, U., Elias, M., Tawfik, D.S.
==See Also==
 
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
Description: Crystal structure of Ancestral variant b9 of SULT 1A1 in complex with PAP and 3-CyC
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Alkolombri U]]
[[Category: Elias M]]
[[Category: Tawfik DS]]

Latest revision as of 15:00, 14 March 2024

Crystal structure of Ancestral variant b9 of SULT 1A1 in complex with PAP and 3-CyCCrystal structure of Ancestral variant b9 of SULT 1A1 in complex with PAP and 3-CyC

Structural highlights

3qvv 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 2.35Å
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

3qvv, resolution 2.35Å

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