3app
From Proteopedia
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==STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION== | ==STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION== | ||
| - | <StructureSection load='3app' size='340' side='right' caption='[[3app]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3app' size='340' side='right'caption='[[3app]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3app]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3app]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_janthinellum Penicillium janthinellum]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2app 2app] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1app 1app]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APP FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3app FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3app OCA], [https://pdbe.org/3app PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3app RCSB], [https://www.ebi.ac.uk/pdbsum/3app PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3app ProSAT]</span></td></tr> |
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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*[[Penicillopepsin|Penicillopepsin]] | *[[Penicillopepsin|Penicillopepsin]] | ||
*[[Pepsin|Pepsin]] | *[[Pepsin|Pepsin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Penicillium janthinellum]] |
| - | [[Category: James | + | [[Category: James MNG]] |
| - | [[Category: Sielecki | + | [[Category: Sielecki AR]] |
Current revision
STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION
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