2aak

<table><tr><td colspan='2'>[[2aak]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1aak 1aak]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AAK FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2aak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aak OCA], [http://pdbe.org/2aak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aak RCSB], [http://www.ebi.ac.uk/pdbsum/2aak PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aak ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/UBC1_ARATH UBC1_ARATH]] Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.<ref>PMID:16339806</ref> <ref>PMID:8386169</ref>

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== Publication Abstract from PubMed ==

The x-ray crystal structure of a recombinant ubiquitin-conjugating enzyme (E2) encoded by the UBC1 gene of the plant Arabidopsis thaliana has been determined with the use of multiple isomorphous replacement techniques and refined at 2.4-A resolution by simulated annealing and restrained least-squares. This E2 is an alpha/beta protein, with four alpha-helices and a four-stranded antiparallel beta-sheet. The NH2 and COOH termini, which may be important for interaction with other enzymes and substrates in the ubiquitin-conjugation pathway, are on the opposite side of the molecule from the cysteine residue that binds to the COOH terminus of ubiquitin. This structure should now allow for the rational analysis of E2 function by in vitro mutagenesis and facilitate the effective design of E2s with unique specificities or catalytic functions.

Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).,Cook WJ, Jeffrey LC, Sullivan ML, Vierstra RD J Biol Chem. 1992 Jul 25;267(21):15116-21. PMID:1321826<ref>PMID:1321826</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2aak" style="background-color:#fffaf0;"></div>

*[[PDB identification code|PDB identification code]]

*[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]]

[[Category: Arath]]

[[Category: Cook, W J]]

[[Category: Jeffrey, L C]]

[[Category: Sullivan, M L]]

[[Category: Vierstra, R D]]

[[Category: Ubiquitin conjugation]]