› 2v31

Solution NMR

Structure of First Catalytic Cysteine Half-domain of mouse ubiquitin- activating enzyme

Released:
DOI: 10.2210/pdb2v31/pdb
PDB entry 2v31 coloured by chain, ensemble of 20 models, front view.
PDB entry 2v31 coloured by chain, ensemble of 20 models, side view.
PDB entry 2v31 coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Entry authors: Jaremko L, Jaremko M, Wojciechowski W, Filipek R, Szczepanowski RH, Bochtler M, Zhukov I

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
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
Refinement method: CYANA

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