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==Crystal structure of human phytanoyl-CoA dioxygenase PHYHD1 (apo)== | ==Crystal structure of human phytanoyl-CoA dioxygenase PHYHD1 (apo)== | ||
<StructureSection load='2opw' size='340' side='right' caption='[[2opw]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2opw' size='340' side='right'caption='[[2opw]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2opw]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2opw]] is a 1 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=2OPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OPW FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHYHD1 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHYHD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2opw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2opw OCA], [https://pdbe.org/2opw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2opw RCSB], [https://www.ebi.ac.uk/pdbsum/2opw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2opw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PHYD1_HUMAN PHYD1_HUMAN]] Isoform 1 has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA. Isoform 2 and isoform 3 probably lack enzyme activity.<ref>PMID:21530488</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bray, J E]] | [[Category: Bray, J E]] |
Revision as of 16:02, 9 June 2021
Crystal structure of human phytanoyl-CoA dioxygenase PHYHD1 (apo)Crystal structure of human phytanoyl-CoA dioxygenase PHYHD1 (apo)
Structural highlights
Function[PHYD1_HUMAN] Isoform 1 has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA. Isoform 2 and isoform 3 probably lack enzyme activity.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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