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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=4lsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lsx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lsx RCSB], [http://www.ebi.ac.uk/pdbsum/4lsx 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=4lsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lsx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lsx RCSB], [http://www.ebi.ac.uk/pdbsum/4lsx PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SERK1_ARATH SERK1_ARATH]] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway.<ref>PMID:11509554</ref> <ref>PMID:17693538</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 14:19, 25 December 2014

Plant steroid receptor ectodomain bound to brassinolide and SERK1 co-receptor ectodomain

4lsx, resolution 3.30Å

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