CATH Classification

Domain Context

CATH Clusters

Superfamily SWIB/MDM2 domain
Functional Family

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q00987
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.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through 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. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31.

UniProtKB Entries (1)

Q00987
MDM2_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase Mdm2

PDB Structure

PDB 5LAW
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Discovery of Novel Spiro[3H-indole-3,2'-pyrrolidin]-2(1H)-one Compounds as Chemically Stable and Orally Active Inhibitors of the MDM2-p53 Interaction.
Gollner, A., Rudolph, D., Arnhof, H., Bauer, M., Blake, S.M., Boehmelt, G., Cockroft, X.L., Dahmann, G., Ettmayer, P., Gerstberger, T., Karolyi-Oezguer, J., Kessler, D., Kofink, C., Ramharter, J., Rinnenthal, J., Savchenko, A., Schnitzer, R., Weinstabl, H., Weyer-Czernilofsky, U., Wunberg, T., McConnell, D.B.
J. Med. Chem.