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.


1eh5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:59, 9 August 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1 COMPLEXED WITH PALMITATE==
==CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1 COMPLEXED WITH PALMITATE==
-
<StructureSection load='1eh5' size='340' side='right' caption='[[1eh5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+
<StructureSection load='1eh5' size='340' side='right'caption='[[1eh5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1eh5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EH5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1eh5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EH5 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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]] 2.5&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ei9|1ei9]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Palmitoyl-protein_hydrolase Palmitoyl-protein hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.22 3.1.2.22] </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=1eh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eh5 OCA], [https://pdbe.org/1eh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eh5 RCSB], [https://www.ebi.ac.uk/pdbsum/1eh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eh5 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=1eh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eh5 OCA], [http://pdbe.org/1eh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eh5 RCSB], [http://www.ebi.ac.uk/pdbsum/1eh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eh5 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PPT1_BOVIN PPT1_BOVIN]] Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
+
[https://www.uniprot.org/uniprot/PPT1_BOVIN PPT1_BOVIN] Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 30: Line 29:
</div>
</div>
<div class="pdbe-citations 1eh5" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1eh5" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bovin]]
+
[[Category: Bos taurus]]
-
[[Category: Palmitoyl-protein hydrolase]]
+
[[Category: Large Structures]]
-
[[Category: Clardy, J]]
+
[[Category: Bellizzi III JJ]]
-
[[Category: Das, A K]]
+
[[Category: Clardy J]]
-
[[Category: Hofmann, S L]]
+
[[Category: Das AK]]
-
[[Category: III, J J.Bellizzi]]
+
[[Category: Hofmann SL]]
-
[[Category: Kemp, C]]
+
[[Category: Kemp C]]
-
[[Category: Lu, J Y]]
+
[[Category: Lu JY]]
-
[[Category: Widom, J]]
+
[[Category: Widom J]]
-
[[Category: Alpha/beta hydrolase]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Hydrolase]]
+

Current revision

CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1 COMPLEXED WITH PALMITATE

PDB ID 1eh5

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/1eh5"
Personal tools