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3c17

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==Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation==
==Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation==
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<StructureSection load='3c17' size='340' side='right' caption='[[3c17]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='3c17' size='340' side='right'caption='[[3c17]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3c17]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C17 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3c17]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C17 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zak|2zak]], [[1k2x|1k2x]], [[1jn9|1jn9]], [[2zal|2zal]], [[1t3m|1t3m]], [[2gez|2gez]], [[9gac|9gac]], [[9gaf|9gaf]], [[9gaa|9gaa]], [[2gac|2gac]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zak|2zak]], [[1k2x|1k2x]], [[1jn9|1jn9]], [[2zal|2zal]], [[1t3m|1t3m]], [[2gez|2gez]], [[9gac|9gac]], [[9gaf|9gaf]], [[9gaa|9gaa]], [[2gac|2gac]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ybiK (iaaA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ybiK (iaaA) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<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=3c17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c17 OCA], [http://pdbe.org/3c17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c17 RCSB], [http://www.ebi.ac.uk/pdbsum/3c17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c17 ProSAT]</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=3c17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c17 OCA], [https://pdbe.org/3c17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c17 RCSB], [https://www.ebi.ac.uk/pdbsum/3c17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c17 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/IAAA_ECOLI IAAA_ECOLI]] Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.<ref>PMID:11988085</ref> May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.<ref>PMID:11988085</ref>
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[[https://www.uniprot.org/uniprot/IAAA_ECOLI IAAA_ECOLI]] Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.<ref>PMID:11988085</ref> May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.<ref>PMID:11988085</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Aminopeptidase|Aminopeptidase]]
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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*[[Asparaginase|Asparaginase]]
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*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Hernandez-Santoyo, A]]
[[Category: Hernandez-Santoyo, A]]
[[Category: Jaskolski, M]]
[[Category: Jaskolski, M]]

Revision as of 07:29, 10 November 2021

Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation

PDB ID 3c17

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