PDBe 2lzj

Solution NMR

Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme

Released:

Function and Biology Details

Reaction catalysed:
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-like modifier-activating enzyme 1 Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.2 KDa
Source organism: Mus musculus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q02053 (Residues: 202-312; Coverage: 11%)
Gene names: Sbx, Uba1, Ube1, Ube1ax, Ube1x
Sequence domains: Ubiquitin-activating enzyme E1 FCCH domain
Structure domains: Elongation Factor Tu (Ef-tu); domain 3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: simulated annealing
Chemical shifts: BMR18758  
Expression system: Saccharomyces cerevisiae