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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]] 1.90&Aring;' scene=''>
<StructureSection load='2opw' size='340' side='right'caption='[[2opw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2opw]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OPW FirstGlance]. <br>
<table><tr><td colspan='2'>[[2opw]] is a 1 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=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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2opw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2opw OCA], [http://pdbe.org/2opw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2opw RCSB], [http://www.ebi.ac.uk/pdbsum/2opw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2opw 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=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 ==
[[http://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>
[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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</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=2opw 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=2opw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H]]
[[Category: Large Structures]]
[[Category: Bray, J E]]
[[Category: Arrowsmith CH]]
[[Category: Butler, D]]
[[Category: Bray JE]]
[[Category: Delft, F von]]
[[Category: Butler D]]
[[Category: Edwards, A]]
[[Category: Edwards A]]
[[Category: Kavanagh, K L]]
[[Category: Kavanagh KL]]
[[Category: McDonough, M A]]
[[Category: McDonough MA]]
[[Category: Ng, S S]]
[[Category: Ng SS]]
[[Category: Oppermann, U]]
[[Category: Oppermann U]]
[[Category: Structural genomic]]
[[Category: Schofield CJ]]
[[Category: Schofield, C J]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Zhang Z]]
[[Category: Zhang, Z]]
[[Category: Von Delft F]]
[[Category: Double-stranded beta helix]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase]]
[[Category: Phyhd1]]
[[Category: Sgc]]

Latest revision as of 03:21, 28 December 2023

Crystal structure of human phytanoyl-CoA dioxygenase PHYHD1 (apo)Crystal structure of human phytanoyl-CoA dioxygenase PHYHD1 (apo)

Structural highlights

2opw is a 1 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 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ Zhang Z, Kochan GT, Ng SS, Kavanagh KL, Oppermann U, Schofield CJ, McDonough MA. Crystal structure of PHYHD1A, a 2OG oxygenase related to phytanoyl-CoA hydroxylase. Biochem Biophys Res Commun. 2011 May 20;408(4):553-8. doi:, 10.1016/j.bbrc.2011.04.059. Epub 2011 Apr 21. PMID:21530488 doi:10.1016/j.bbrc.2011.04.059

2opw, resolution 1.90Å

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