2lzj | pdb_00002lzj
From Proteopedia
Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme
Template:ABSTRACT PUBMED 24211821
Function
[UBA1_MOUSE] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP.
About this Structure
2lzj is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA.
Reference
- Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A. NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme. J Struct Biol. 2013 Nov 6. pii: S1047-8477(13)00299-2. doi:, 10.1016/j.jsb.2013.10.020. PMID:24211821 doi:https://dx.doi.org/10.1016/j.jsb.2013.10.020
