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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]] 1.80&Aring;' scene=''>
<StructureSection load='3app' size='340' side='right'caption='[[3app]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3app]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_340.48 Cbs 340.48]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3APP FirstGlance]. <br>
<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillopepsin Penicillopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.20 3.4.23.20] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<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=3app FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3app OCA], [http://pdbe.org/3app PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3app RCSB], [http://www.ebi.ac.uk/pdbsum/3app PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3app 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=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: Cbs 340 48]]
[[Category: Large Structures]]
[[Category: Penicillopepsin]]
[[Category: Penicillium janthinellum]]
[[Category: James, M N.G]]
[[Category: James MNG]]
[[Category: Sielecki, A R]]
[[Category: Sielecki AR]]

Latest revision as of 08:40, 5 June 2024

STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTIONSTRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION

Structural highlights

3app is a 1 chain structure with sequence from Penicillium janthinellum. This structure supersedes the now removed PDB entries 2app and 1app. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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'.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Mains G, Takahashi M, Sodek J, Hofmann T. The specificity of penicillopepsin. Can J Biochem. 1971 Oct;49(10):1134-49. PMID:4946839 doi:10.1139/o71-164

3app, resolution 1.80Å

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