CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

2.3.2.23
E2 ubiquitin-conjugating enzyme.
based on mapping to UniProt P61088
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 (2)

Q0PF16
TRIM5_MACMU
Macaca mulatta
Tripartite motif-containing protein 5
P61088
UBE2N_HUMAN
Homo sapiens
Ubiquitin-conjugating enzyme E2 N

PDB Structure

PDB 4TKP
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Activation of the Ubc13-Ub adduct by the RING domain of the TRIM5alpha retroviral restriction factor offers insight into the mechanism of molecular pattern recognition by TRIM proteins
Yudina, Z., Johnson, R., Roa, A., Biris, N., Tsiperson, V., Taylor, A.B., Hart, P.J., Demeler, B., Diaz-Griffero, F., Ivanov, D.N.
Cell Rep
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