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The structure of the ubiquitin conjugating enzyme (E2) UbcH5B has been solved by a combination of homology modeling, diffusion anisotropy derived from NMR relaxation data and automated NOE assignment. Comparison with E2 structures present in the PDB and solved previously by X-ray crystallography or NMR shows in all cases the same compact fold. Differences are observed in the orientation of both the C-terminal α-helices and the N-terminal α-helix that is known to be involved in binding to the ubiquitin ligase (E3). In addition, the side chain of a conserved asparagine residue (Asn77), that is near the active site cysteine and that has been shown to be important for isopeptide bond formation, is solvent exposed. This positioning supports the proposed catalytic function of this amino acid (Wu et al., 2003).

NMR solution structure of the E2 ubiquitin conjugating enzyme UbcH5B