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1fy2

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{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
 
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===Aspartyl Dipeptidase===
 
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{{ABSTRACT_PUBMED_11106384}}
 
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==Function==
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==Aspartyl Dipeptidase==
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[[http://www.uniprot.org/uniprot/PEPE_SALTY PEPE_SALTY]] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]
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<StructureSection load='1fy2' size='340' side='right'caption='[[1fy2]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fy2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FY2 FirstGlance]. <br>
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[[1fy2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA].
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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]] 1.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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==Reference==
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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=1fy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fy2 OCA], [https://pdbe.org/1fy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fy2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fy2 ProSAT]</span></td></tr>
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<ref group="xtra">PMID:011106384</ref><references group="xtra"/><references/>
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</table>
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
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== Function ==
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[[Category: Hakansson, K.]]
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[https://www.uniprot.org/uniprot/PEPE_SALTY PEPE_SALTY] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]
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[[Category: Miller, C G.]]
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== Evolutionary Conservation ==
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[[Category: Wang, A H.J.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Catalytic triad]]
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Check<jmol>
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[[Category: Hydrolase]]
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<jmolCheckbox>
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[[Category: Peptidase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fy2_consurf.spt"</scriptWhenChecked>
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[[Category: Serine protease]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Strand-helix motif]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fy2 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Hakansson K]]
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[[Category: Miller CG]]
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[[Category: Wang AH-J]]

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Aspartyl Dipeptidase

PDB ID 1fy2

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