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.


2zl3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of H.pylori ClpP S99A==
==Crystal structure of H.pylori ClpP S99A==
-
<StructureSection load='2zl3' size='340' side='right' caption='[[2zl3]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+
<StructureSection load='2zl3' size='340' side='right'caption='[[2zl3]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2zl3]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZL3 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2zl3]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZL3 FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zl0|2zl0]], [[2zl2|2zl2]], [[2zl4|2zl4]]</td></tr>
+
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zl0|2zl0]], [[2zl2|2zl2]], [[2zl4|2zl4]]</div></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>
+
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </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=2zl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zl3 OCA], [http://pdbe.org/2zl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zl3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zl3 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=2zl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zl3 OCA], [https://pdbe.org/2zl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zl3 RCSB], [https://www.ebi.ac.uk/pdbsum/2zl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zl3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/CLPP_HELPY CLPP_HELPY]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
+
[[https://www.uniprot.org/uniprot/CLPP_HELPY CLPP_HELPY]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 32: Line 32:
==See Also==
==See Also==
-
*[[Clp Protease|Clp Protease]]
+
*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 39: Line 39:
[[Category: Atcc 43504]]
[[Category: Atcc 43504]]
[[Category: Endopeptidase Clp]]
[[Category: Endopeptidase Clp]]
 +
[[Category: Large Structures]]
[[Category: Kim, D Y]]
[[Category: Kim, D Y]]
[[Category: Kim, K K]]
[[Category: Kim, K K]]

Revision as of 07:17, 10 November 2021

Crystal structure of H.pylori ClpP S99A

PDB ID 2zl3

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/2zl3"
Personal tools