3dyd

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Current revision (12:55, 30 August 2023) (edit) (undo)
 
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<StructureSection load='3dyd' size='340' side='right'caption='[[3dyd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3dyd' size='340' side='right'caption='[[3dyd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3dyd]] 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=3DYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3dyd]] 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=3DYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYD 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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAT ([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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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/Tyrosine_transaminase Tyrosine transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.5 2.6.1.5] </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=3dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyd OCA], [https://pdbe.org/3dyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dyd RCSB], [https://www.ebi.ac.uk/pdbsum/3dyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyd 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=3dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyd OCA], [https://pdbe.org/3dyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dyd RCSB], [https://www.ebi.ac.uk/pdbsum/3dyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyd ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN]] Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:[https://omim.org/entry/276600 276600]]; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.<ref>PMID:1357662</ref>
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[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN] Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:[https://omim.org/entry/276600 276600]; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.<ref>PMID:1357662</ref>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN]] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.<ref>PMID:7999802</ref> <ref>PMID:16640556</ref>
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[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.<ref>PMID:7999802</ref> <ref>PMID:16640556</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: Tyrosine transaminase]]
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[[Category: Andersson J]]
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[[Category: Andersson, J]]
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[[Category: Arrowsmith CH]]
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[[Category: Arrowsmith, C H]]
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[[Category: Berglund H]]
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[[Category: Berg, S Van Den]]
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[[Category: Collins R]]
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[[Category: Berglund, H]]
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[[Category: Dahlgren LG]]
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[[Category: Collins, R]]
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[[Category: Edwards AM]]
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[[Category: Dahlgren, L G]]
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[[Category: Flodin S]]
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[[Category: Edwards, A M]]
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[[Category: Flores A]]
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[[Category: Flodin, S]]
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[[Category: Graslund S]]
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[[Category: Flores, A]]
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[[Category: Hammarstrom M]]
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[[Category: Graslund, S]]
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[[Category: Johansson A]]
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[[Category: Hammarstrom, M]]
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[[Category: Johansson I]]
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[[Category: Johansson, A]]
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[[Category: Karlberg T]]
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[[Category: Johansson, I]]
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[[Category: Kotenyova T]]
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[[Category: Karlberg, T]]
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[[Category: Lehtio L]]
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[[Category: Kotenyova, T]]
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[[Category: Moche M]]
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[[Category: Lehtio, L]]
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[[Category: Nilsson ME]]
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[[Category: Moche, M]]
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[[Category: Nordlund P]]
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[[Category: Nilsson, M E]]
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[[Category: Nyman T]]
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[[Category: Nordlund, P]]
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[[Category: Olesen K]]
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[[Category: Nyman, T]]
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[[Category: Persson C]]
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[[Category: Olesen, K]]
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[[Category: Sagemark J]]
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[[Category: Persson, C]]
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[[Category: Schuler H]]
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[[Category: Structural genomic]]
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[[Category: Thorsell AG]]
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[[Category: Sagemark, J]]
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[[Category: Tresaugues L]]
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[[Category: Schuler, H]]
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[[Category: Van Den Berg S]]
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[[Category: Thorsell, A G]]
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[[Category: Weigelt J]]
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[[Category: Tresaugues, L]]
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[[Category: Welin M]]
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[[Category: Weigelt, J]]
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[[Category: Wikstrom M]]
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[[Category: Welin, M]]
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[[Category: Wisniewska M]]
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[[Category: Wikstrom, M]]
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[[Category: Wisniewska, M]]
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[[Category: Aminotransferase]]
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[[Category: Disease mutation]]
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[[Category: Phenylalanine catabolism]]
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[[Category: Plp]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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[[Category: Tyrosine]]
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[[Category: Tyrosine catabolism]]
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Current revision

Human Tyrosine Aminotransferase

PDB ID 3dyd

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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