2aak

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UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANAUBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA

Structural highlights

2aak is a 1 chain structure with sequence from Arabidopsis thaliana. This structure supersedes the now removed PDB entry 1aak. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UBC1_ARATH Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Kraft E, Stone SL, Ma L, Su N, Gao Y, Lau OS, Deng XW, Callis J. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol. 2005 Dec;139(4):1597-611. PMID:16339806 doi:http://dx.doi.org/139/4/1597
  2. ↑ Sullivan ML, Vierstra RD. Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+. J Biol Chem. 1993 Apr 25;268(12):8777-80. PMID:8386169

2aak, resolution 2.40Å

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