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4omd

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Current revision (07:32, 25 January 2023) (edit) (undo)
 
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==X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba==
==X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba==
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<StructureSection load='4omd' size='340' side='right' caption='[[4omd]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='4omd' size='340' side='right'caption='[[4omd]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4omd]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OMD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4omd]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</scene></td></tr>
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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=4omd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omd OCA], [https://pdbe.org/4omd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omd RCSB], [https://www.ebi.ac.uk/pdbsum/4omd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omd ProSAT]</span></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4omc|4omc]], [[1p8j|1p8j]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FURIN, FUR, PACE, PCSK3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Furin Furin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.75 3.4.21.75] </span></td></tr>
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<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=4omd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omd OCA], [http://pdbe.org/4omd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4omd RCSB], [http://www.ebi.ac.uk/pdbsum/4omd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4omd ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FURIN_HUMAN FURIN_HUMAN]] Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.<ref>PMID:7690548</ref>
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[https://www.uniprot.org/uniprot/FURIN_HUMAN FURIN_HUMAN] Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.<ref>PMID:7690548</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Furin]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Dahms, S O]]
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[[Category: Dahms SO]]
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[[Category: Than, M E]]
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[[Category: Than ME]]
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[[Category: Competitive inhibitor]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Pro-protein convertase]]
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[[Category: Protease-inhibitor complex]]
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[[Category: Serine protease]]
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Current revision

X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba

PDB ID 4omd

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