CATH Classification

Domain Context

CATH Clusters

Superfamily Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1
Functional Family ubiquitin-like modifier-activating enzyme 1

Enzyme Information

6.2.1.45
E1 ubiquitin-activating enzyme.
based on mapping to UniProt P22314
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.
-!- Catalyzes the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. -!- The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.

UniProtKB Entries (1)

P62979
RS27A_HUMAN
Homo sapiens
Ubiquitin-40S ribosomal protein S27a

PDB Structure

PDB 6DC6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of a human ubiquitin E1-ubiquitin complex reveals conserved functional elements essential for activity.
Lv, Z., Williams, K.M., Yuan, L., Atkison, J.H., Olsen, S.K.
J. Biol. Chem.