4o2w: Difference between revisions

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-'''Unreleased structure'''
-The entry 4o2w is ON HOLD
+==Crystal structure of the third RCC1-like domain of HERC1==
+<StructureSection load='4o2w' size='340' side='right'caption='[[4o2w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4o2w]] is a 4 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=4O2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O2W FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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=4o2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o2w OCA], [https://pdbe.org/4o2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o2w RCSB], [https://www.ebi.ac.uk/pdbsum/4o2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o2w ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HERC1_HUMAN HERC1_HUMAN] Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.<ref>PMID:8861955</ref> <ref>PMID:9233772</ref> <ref>PMID:15642342</ref>
-Authors: DONG, A., HU, J., LI, Y., WALKER, J.R., Bountra, C., Arrowsmith, C.H., Edwards, A.M., TONG, Y., Structural Genomics Consortium (SGC)
+==See Also==
+*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
-Description: Crystal structure of the third RCC1-like domain of HERC1
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Arrowsmith CH]]
+[[Category: Bountra C]]
+[[Category: Dong A]]
+[[Category: Edwards AM]]
+[[Category: Hu J]]
+[[Category: Li Y]]
+[[Category: Tong Y]]
+[[Category: Walker JR]]