CATH Classification

Domain Context

CATH Clusters

Superfamily Ubiquitin Conjugating Enzyme
Functional Family Ubiquitin-conjugating enzyme E2 W

Enzyme Information

2.3.2.25
N-terminal E2 ubiquitin-conjugating enzyme.
based on mapping to UniProt Q96B02
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L- cysteine + N-terminal-ubiquitinyl-[acceptor protein].
-!- The enzyme ubiquitinylates the N-terminus of the acceptor protein. -!- It is not reactive toward free lysine.
2.3.2.23
E2 ubiquitin-conjugating enzyme.
based on mapping to UniProt Q96B02
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine.
-!- The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. -!- In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage. -!- Formerly EC 6.3.2.19.

UniProtKB Entries (1)

Q96B02
UBE2W_HUMAN
Homo sapiens
Ubiquitin-conjugating enzyme E2 W

PDB Structure

PDB 2MT6
External Links
Method SOLUTION NMR
Organism
Primary Citation
Intrinsic disorder drives N-terminal ubiquitination by Ube2w.
Vittal, V., Shi, L., Wenzel, D.M., Scaglione, K.M., Duncan, E.D., Basrur, V., Elenitoba-Johnson, K.S., Baker, D., Paulson, H.L., Brzovic, P.S., Klevit, R.E.
Nat.Chem.Biol.