6teu
From Proteopedia
(Difference between revisions)
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==Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Val80Lys mutant - Cocrystal with Fe2+, Mn2+== | ==Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Val80Lys mutant - Cocrystal with Fe2+, Mn2+== | ||
| - | <StructureSection load='6teu' size='340' side='right'caption='[[6teu]]' scene=''> | + | <StructureSection load='6teu' size='340' side='right'caption='[[6teu]], [[Resolution|resolution]] 3.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TEU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6teu]] 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=6TEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TEU FirstGlance]. <br> |
| - | </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=6teu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6teu OCA], [https://pdbe.org/6teu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6teu RCSB], [https://www.ebi.ac.uk/pdbsum/6teu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6teu ProSAT]</span></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]] 3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6teu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6teu OCA], [https://pdbe.org/6teu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6teu RCSB], [https://www.ebi.ac.uk/pdbsum/6teu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6teu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/PLOD3_HUMAN PLOD3_HUMAN] Connective tissue disorder due to lysyl hydroxylase-3 deficiency. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PLOD3_HUMAN PLOD3_HUMAN] Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.[UniProtKB:P24802] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chiapparino A]] | [[Category: Chiapparino A]] | ||
Revision as of 06:17, 19 July 2023
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Val80Lys mutant - Cocrystal with Fe2+, Mn2+
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