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1yjl
From Proteopedia
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==Reduced Peptidylglycine alpha-Hydroxylating Monooxygenase in a new crystal form== | ==Reduced Peptidylglycine alpha-Hydroxylating Monooxygenase in a new crystal form== | ||
| - | <StructureSection load='1yjl' size='340' side='right' caption='[[1yjl]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1yjl' size='340' side='right'caption='[[1yjl]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1yjl]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1yjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJL FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=1yjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjl OCA], [https://pdbe.org/1yjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yjl RCSB], [https://www.ebi.ac.uk/pdbsum/1yjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjl ProSAT]</span></td></tr> | |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yj/1yjl_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yj/1yjl_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1yjl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1yjl" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Amzel | + | [[Category: Amzel LM]] |
| - | [[Category: Blackburn | + | [[Category: Blackburn NJ]] |
| - | [[Category: Eipper | + | [[Category: Eipper BA]] |
| - | [[Category: Mains | + | [[Category: Mains RE]] |
| - | [[Category: Prigge | + | [[Category: Prigge ST]] |
| - | [[Category: Siebert | + | [[Category: Siebert X]] |
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Current revision
Reduced Peptidylglycine alpha-Hydroxylating Monooxygenase in a new crystal form
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