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2h11

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Current revision (09:50, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2h11' size='340' side='right'caption='[[2h11]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
<StructureSection load='2h11' size='340' side='right'caption='[[2h11]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2h11]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H11 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2h11]] 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=2H11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H11 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></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]] 1.89&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPMT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiopurine_S-methyltransferase Thiopurine S-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.67 2.1.1.67] </span></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=2h11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h11 OCA], [https://pdbe.org/2h11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h11 RCSB], [https://www.ebi.ac.uk/pdbsum/2h11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h11 ProSAT]</span></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=2h11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h11 OCA], [https://pdbe.org/2h11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h11 RCSB], [https://www.ebi.ac.uk/pdbsum/2h11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h11 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN]] Defects in TPMT are the cause of thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:[https://omim.org/entry/610460 610460]]. TPMT is an enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosupressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus.
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[https://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN] Defects in TPMT are the cause of thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:[https://omim.org/entry/610460 610460]. TPMT is an enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosupressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN]] Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.<ref>PMID:18484748</ref>
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[https://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN] Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.<ref>PMID:18484748</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thiopurine S-methyltransferase]]
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[[Category: Cheng X]]
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[[Category: Cheng, X]]
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[[Category: Horton JR]]
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[[Category: Horton, J R]]
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[[Category: Binary protein-cofactor complex]]
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[[Category: Transferase]]
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Current revision

Amino-terminal Truncated Thiopurine S-Methyltransferase Complexed with S-Adenosyl-L-Homocysteine

PDB ID 2h11

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OCA

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