CATH Classification

Domain Context

CATH Clusters

Superfamily Periplasmic binding protein-like II
Functional Family Maltose/maltodextrin-binding periplasmic protein

Enzyme Information

2.3.2.26
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt Q05086
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. -!- In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon- amino group of an L-lysine residue of the acceptor protein. -!- Cf. EC 2.3.2.27 and EC 2.3.2.31.

UniProtKB Entries (3)

P0AEX9
MALE_ECOLI
Escherichia coli K-12
Maltose/maltodextrin-binding periplasmic protein
Q05086
UBE3A_HUMAN
Homo sapiens
Ubiquitin-protein ligase E3A
P03126
VE6_HPV16
Human papillomavirus type 16
Protein E6

PDB Structure

PDB 4GIZ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins.
Zanier, K., Charbonnier, S., Sidi, A.O., McEwen, A.G., Ferrario, M.G., Poussin-Courmontagne, P., Cura, V., Brimer, N., Babah, K.O., Ansari, T., Muller, I., Stote, R.H., Cavarelli, J., Vande Pol, S., Trave, G.
Science