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 5OC8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Dose and Schedule Determine Distinct Molecular Mechanisms Underlying the Efficacy of the p53-MDM2 Inhibitor HDM201.
Jeay, S., Ferretti, S., Holzer, P., Fuchs, J., Chapeau, E.A., Wartmann, M., Sterker, D., Romanet, V., Murakami, M., Kerr, G., Durand, E.Y., Gaulis, S., Cortes-Cros, M., Ruetz, S., Stachyra, T.M., Kallen, J., Furet, P., Wurthner, J., Guerreiro, N., Halilovic, E., Jullion, A., Kauffmann, A., Kuriakose, E., Wiesmann, M., Jensen, M.R., Hofmann, F., Sellers, W.R.
Cancer Res.
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