2h6j

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Current revision (09:52, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2h6j' size='340' side='right'caption='[[2h6j]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='2h6j' size='340' side='right'caption='[[2h6j]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2h6j]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H6J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2h6j]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H6J FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prcA 1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928]), prcB 1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6j OCA], [https://pdbe.org/2h6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h6j RCSB], [https://www.ebi.ac.uk/pdbsum/2h6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h6j 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=2h6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6j OCA], [https://pdbe.org/2h6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h6j RCSB], [https://www.ebi.ac.uk/pdbsum/2h6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h6j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PSA1_RHOER PSA1_RHOER]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.[HAMAP-Rule:MF_00289]<ref>PMID:7583123</ref> <ref>PMID:9000518</ref> [[https://www.uniprot.org/uniprot/PSB1_RHOER PSB1_RHOER]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.[HAMAP-Rule:MF_02113]<ref>PMID:7583123</ref> <ref>PMID:9000518</ref>
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[https://www.uniprot.org/uniprot/PSA1_RHOER PSA1_RHOER] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.[HAMAP-Rule:MF_00289]<ref>PMID:7583123</ref> <ref>PMID:9000518</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycobacterium erythropolis gray and thornton 1928]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Proteasome endopeptidase complex]]
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[[Category: Rhodococcus erythropolis]]
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[[Category: Kwon, Y D]]
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[[Category: Kwon YD]]
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[[Category: 20s proteasome]]
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[[Category: Assembly-dependent activation]]
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[[Category: Half proteasome]]
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[[Category: Hydrolase]]
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Current revision

Crystal Structure of the Beta F145A Rhodococcus Proteasome

PDB ID 2h6j

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