7oik

Electron Microscopy
3.5Å resolution

Mouse RNF213:UBE2L3 transthiolation intermediate, chemically stabilized

Released:
Source organisms:
Entry authors: Grabarczyk D, Ahel J, Clausen T
Related structures: EMD-12931

Function and Biology Details

Reactions catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-123220 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RNF213 Chain: A
Molecule details ›
Chain: A
Length: 5161 amino acids
Theoretical weight: 586.55 KDa
Source organism: Mus musculus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: E9Q555 (Residues: 1-5148; Coverage: 100%)
Gene names: Mystr, Rnf213
Sequence domains:
Ubiquitin-conjugating enzyme E2 L3 Chain: B
Molecule details ›
Chain: B
Length: 166 amino acids
Theoretical weight: 19.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P68036 (Residues: 1-154; Coverage: 100%)
Gene names: UBCE7, UBCH7, UBE2L3
Sequence domains: Ubiquitin-conjugating enzyme

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.5Å
Relevant EMDB volumes: EMD-12931
Expression systems:
  • Trichoplusia ni
  • Escherichia coli BL21(DE3)