5v86

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m (Protected "5v86" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5v86 is ON HOLD
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==Structure of DCN1 bound to NAcM-OPT==
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<StructureSection load='5v86' size='340' side='right'caption='[[5v86]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5v86]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V86 FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.374&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8ZA:N-BENZYL-N-(1-BUTYLPIPERIDIN-4-YL)-N-(3,4-DICHLOROPHENYL)UREA'>8ZA</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=5v86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v86 OCA], [https://pdbe.org/5v86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v86 RCSB], [https://www.ebi.ac.uk/pdbsum/5v86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v86 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DCNL1_HUMAN DCNL1_HUMAN] Part of an E3 ubiquitin ligase complex for neddylation. Required for neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes by enhancing the rate of cullins neddylation. Functions to recruit the NEDD8-charged E2 enzyme to the cullin component. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity).[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia virus T4]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Guy RK]]
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[[Category: Hammill JT]]
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[[Category: Schulman BA]]
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[[Category: Scott DC]]

Current revision

Structure of DCN1 bound to NAcM-OPT

PDB ID 5v86

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