3dyd
From Proteopedia
(Difference between revisions)
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==Human Tyrosine Aminotransferase== | ==Human Tyrosine Aminotransferase== | ||
| - | <StructureSection load='3dyd' size='340' side='right' caption='[[3dyd]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3dyd' size='340' side='right'caption='[[3dyd]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dyd]] is a 2 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAT ([ | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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 == | ||
| - | [[ | + | [[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 == | ||
| - | [[ | + | [[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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dyd ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dyd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Tyrosine transaminase]] | [[Category: Tyrosine transaminase]] | ||
[[Category: Andersson, J]] | [[Category: Andersson, J]] | ||
Revision as of 08:10, 9 February 2022
Human Tyrosine Aminotransferase
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Categories: Human | Large Structures | Tyrosine transaminase | Andersson, J | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Collins, R | Dahlgren, L G | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Johansson, A | Johansson, I | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nilsson, M E | Nordlund, P | Nyman, T | Olesen, K | Persson, C | Structural genomic | Sagemark, J | Schuler, H | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, M | Wikstrom, M | Wisniewska, M | Aminotransferase | Disease mutation | Phenylalanine catabolism | Plp | Pyridoxal phosphate | Sgc | Transferase | Tyrosine | Tyrosine catabolism
