1apt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='1apt' size='340' side='right'caption='[[1apt]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1apt' size='340' side='right'caption='[[1apt]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1apt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_340.48 Cbs 340.48]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APT FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1apt]] 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=1APT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APT FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=LTA:4,8-DIAMINO-3-HYDROXY-OCTANOIC+ACID+ETHYL+ESTER'>LTA</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=LTA:4,8-DIAMINO-3-HYDROXY-OCTANOIC+ACID+ETHYL+ESTER'>LTA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1apu|1apu]], [[1apv|1apv]], [[1apw|1apw]]</div></td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Penicillopepsin Penicillopepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.20 3.4.23.20] </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=1apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apt OCA], [https://pdbe.org/1apt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apt RCSB], [https://www.ebi.ac.uk/pdbsum/1apt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apt 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=1apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apt OCA], [https://pdbe.org/1apt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apt RCSB], [https://www.ebi.ac.uk/pdbsum/1apt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apt 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]]
Line 24: Line 24:
*[[Penicillopepsin|Penicillopepsin]]
*[[Penicillopepsin|Penicillopepsin]]
*[[Pepsin|Pepsin]]
*[[Pepsin|Pepsin]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Cbs 340 48]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Penicillopepsin]]
+
[[Category: Penicillium janthinellum]]
-
[[Category: James, M N.G]]
+
[[Category: James MNG]]
-
[[Category: Sielecki, A R]]
+
[[Category: Sielecki AR]]
-
[[Category: Acid proteinase]]
+
-
[[Category: Hydrolase-hydrolase inhibitor complex]]
+

Revision as of 15:27, 13 March 2024

CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE BINDING TO THE ASPARTYL PROTEINASE PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION

PDB ID 1apt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools