› 2lzj

Solution NMR

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

Released:
DOI: 10.2210/pdb2lzj/pdb
PDB entry 2lzj coloured by chain, ensemble of 20 models, front view.
PDB entry 2lzj coloured by chain, ensemble of 20 models, side view.
PDB entry 2lzj coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Jaremko M, Jaremko Ł, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A
J Struct Biol 185 69-78 (2014)
PMID: 24211821

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169661 (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: Ubiquitin-activating enzyme E1, FCCH domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 94%
Refinement method: simulated annealing
Expression system: Saccharomyces cerevisiae

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Citations

2 citation in other articles

Fast evaluation of protein dynamics from deficient 15N relaxation data.
Jaremko et al. (2018)
1 more