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==Crystal structure of peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase complex with Pro-Pro-Gly-Pro-Ala-Gly-Pro-Pro-Gly.==
==Crystal structure of peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase complex with Pro-Pro-Gly-Pro-Ala-Gly-Pro-Pro-Gly.==
<StructureSection load='6evn' size='340' side='right' caption='[[6evn]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
<StructureSection load='6evn' size='340' side='right'caption='[[6evn]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6evn]] is a 2 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=6EVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EVN FirstGlance]. <br>
<table><tr><td colspan='2'>[[6evn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EVN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.48&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6evl|6evl]], [[6evm|6evm]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P4HA2, UNQ290/PRO330 ([http://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'>[https://proteopedia.org/fgij/fg.htm?mol=6evn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evn OCA], [https://pdbe.org/6evn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6evn RCSB], [https://www.ebi.ac.uk/pdbsum/6evn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6evn ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Procollagen-proline_dioxygenase Procollagen-proline dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.2 1.14.11.2] </span></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=6evn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evn OCA], [http://pdbe.org/6evn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6evn RCSB], [http://www.ebi.ac.uk/pdbsum/6evn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6evn ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/P4HA2_HUMAN P4HA2_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/P4HA2_HUMAN P4HA2_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/P4HA2_HUMAN P4HA2_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.  
[https://www.uniprot.org/uniprot/P4HA2_HUMAN P4HA2_HUMAN] Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6evn" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6evn" style="background-color:#fffaf0;"></div>
==See Also==
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Procollagen-proline dioxygenase]]
[[Category: Large Structures]]
[[Category: Koski, M K]]
[[Category: Synthetic construct]]
[[Category: Murthy, A V]]
[[Category: Koski MK]]
[[Category: Sulu, R]]
[[Category: Murthy AV]]
[[Category: Wierenga, R K]]
[[Category: Sulu R]]
[[Category: Collagen synthesis]]
[[Category: Wierenga RK]]
[[Category: Hydrolase]]
[[Category: Prolyl 4-hydroxylase]]
[[Category: Tetratricopeptide repeat]]

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