9j78

Electron Microscopy
3.88Å resolution

Cryo-EM structure of CRL2-FEM1B (dimer 2)

Released:
Source organism: Homo sapiens
Related structures: EMD-61197

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-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-291669 (preferred)
Entry contents:
7 distinct polypeptide molecules
Macromolecules (7 distinct):
Elongin-B Chains: D, H
Molecule details ›
Chains: D, H
Length: 121 amino acids
Theoretical weight: 13.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15370 (Residues: 1-118; Coverage: 100%)
Gene names: ELOB, TCEB2
Sequence domains: Ubiquitin family
Cullin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 750 amino acids
Theoretical weight: 87.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13617 (Residues: 2-745; Coverage: 98%)
Gene name: CUL2
Sequence domains:
Elongin-C Chains: C, G
Protein fem-1 homolog B Chains: F, J
E3 ubiquitin-protein ligase RBX1, N-terminally processed Chains: E, I
Poly-UNK Chain: K
Poly-UNK Chain: L

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.88Å
Relevant EMDB volumes: EMD-61197
Expression system: Escherichia coli