1apu: Difference between revisions
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==Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution== | |||
<StructureSection load='1apu' size='340' side='right'caption='[[1apu]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1apu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_janthinellum Penicillium janthinellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=32L:ETHYL+(3S,4S)-4-AMINO-3-HYDROXY-6-METHYLHEPTANOATE'>32L</scene>, <scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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=1apu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apu OCA], [https://pdbe.org/1apu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apu RCSB], [https://www.ebi.ac.uk/pdbsum/1apu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PEPA1_PENJA PEPA1_PENJA] Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'.<ref>PMID:4946839</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apu_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1apu ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Penicillopepsin|Penicillopepsin]] | |||
*[[Pepsin|Pepsin]] | |||
== | == References == | ||
<references/> | |||
[[ | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: | [[Category: Penicillium janthinellum]] | ||
[[Category: | [[Category: James MNG]] | ||
[[Category: | [[Category: Sielecki AR]] | ||
[[Category: | |||
Latest revision as of 04:22, 17 October 2024
Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution
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