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.


1qfm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (23:47, 27 December 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='1qfm' size='340' side='right'caption='[[1qfm]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='1qfm' size='340' side='right'caption='[[1qfm]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1qfm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QFM FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1qfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFM FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SGL:1-HYDROXY-1-THIO-GLYCEROL'>SGL</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</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]] 1.4&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SGL:1-HYDROXY-1-THIO-GLYCEROL'>SGL</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1qfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfm OCA], [https://pdbe.org/1qfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfm RCSB], [https://www.ebi.ac.uk/pdbsum/1qfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfm ProSAT]</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=1qfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfm OCA], [http://pdbe.org/1qfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qfm RCSB], [http://www.ebi.ac.uk/pdbsum/1qfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfm ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG]] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
+
[https://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 38: Line 37:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Prolyl oligopeptidase]]
 
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Fulop, V]]
+
[[Category: Fulop V]]
-
[[Category: Alpha/beta-hydrolase]]
+
-
[[Category: Amnesia]]
+
-
[[Category: Beta-propeller]]
+
-
[[Category: Hydrolase]]
+

Current revision

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE

PDB ID 1qfm

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/1qfm"
Personal tools