This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1g0v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='1g0v' size='340' side='right'caption='[[1g0v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1g0v' size='340' side='right'caption='[[1g0v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1g0v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0V FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1g0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0V 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=MAN:ALPHA-D-MANNOSE'>MAN</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=MAN:ALPHA-D-MANNOSE'>MAN</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">[[1dpj|1dpj]], [[1dp5|1dp5]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dpj|1dpj]], [[1dp5|1dp5]]</div></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>
+
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0v OCA], [http://pdbe.org/1g0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0v RCSB], [http://www.ebi.ac.uk/pdbsum/1g0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0v 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=1g0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0v OCA], [https://pdbe.org/1g0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0v RCSB], [https://www.ebi.ac.uk/pdbsum/1g0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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. [[http://www.uniprot.org/uniprot/IPA3_YEAST IPA3_YEAST]] Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
+
[[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. [[https://www.uniprot.org/uniprot/IPA3_YEAST IPA3_YEAST]] Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 34: Line 34:
*[[Pepsin|Pepsin]]
*[[Pepsin|Pepsin]]
*[[Proteinase|Proteinase]]
*[[Proteinase|Proteinase]]
 +
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>

Revision as of 11:17, 28 July 2021

THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT, MVV

PDB ID 1g0v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g0v"
Personal tools