2lq7

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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=2lq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lq7 RCSB], [http://www.ebi.ac.uk/pdbsum/2lq7 PDBsum]</span></td></tr>
<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=2lq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lq7 RCSB], [http://www.ebi.ac.uk/pdbsum/2lq7 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/UBA3_HUMAN UBA3_HUMAN]] Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.<ref>PMID:10207026</ref> <ref>PMID:9694792</ref> <ref>PMID:12740388</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 18:17, 24 December 2014

E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition

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