4o2w: Difference between revisions
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== | ==Crystal structure of the third RCC1-like domain of HERC1== | ||
[[http://www.uniprot.org/uniprot/HERC1_HUMAN HERC1_HUMAN | <StructureSection load='4o2w' size='340' side='right'caption='[[4o2w]], [[Resolution|resolution]] 2.00Å' 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]] 2Å</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> | |||
== | ==See Also== | ||
[[ | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
== References == | |||
== | <references/> | ||
<references | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: | [[Category: Bountra C]] | ||
[[Category: | [[Category: Dong A]] | ||
[[Category: | [[Category: Edwards AM]] | ||
[[Category: | [[Category: Hu J]] | ||
[[Category: | [[Category: Li Y]] | ||
[[Category: | [[Category: Tong Y]] | ||
[[Category: Walker JR]] | |||
Latest revision as of 20:06, 20 September 2023
Crystal structure of the third RCC1-like domain of HERC1Crystal structure of the third RCC1-like domain of HERC1
Structural highlights
FunctionHERC1_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.[1] [2] [3] See AlsoReferences
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