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1fmx
From Proteopedia
(Difference between revisions)
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<StructureSection load='1fmx' size='340' side='right'caption='[[1fmx]], [[Resolution|resolution]] 2.61Å' scene=''> | <StructureSection load='1fmx' size='340' side='right'caption='[[1fmx]], [[Resolution|resolution]] 2.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1fmx]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1fmx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fmu|1fmu]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fmu|1fmu]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></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=1fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmx OCA], [https://pdbe.org/1fmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmx RCSB], [https://www.ebi.ac.uk/pdbsum/1fmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmx ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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*[[Pepsin|Pepsin]] | *[[Pepsin|Pepsin]] | ||
*[[Proteinase|Proteinase]] | *[[Proteinase|Proteinase]] | ||
| + | *[[Proteinase 3D structures|Proteinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:11, 28 July 2021
STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21
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