2mp2

Solution NMR

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4

Released:

Function and Biology Details

Reaction 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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-157324 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Small ubiquitin-related modifier 3 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55854 (Residues: 12-92; Coverage: 79%)
Gene names: SMT3A, SMT3H1, SUMO3
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Small ubiquitin-related modifier 3 Chain: B
Molecule details ›
Chain: B
Length: 90 amino acids
Theoretical weight: 10.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55854 (Residues: 2-90; Coverage: 86%)
Gene names: SMT3A, SMT3H1, SUMO3
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
E3 ubiquitin-protein ligase RNF4 Chain: C
Molecule details ›
Chain: C
Length: 25 amino acids
Theoretical weight: 2.71 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q9QZS2 (Residues: 45-69; Coverage: 13%)
Gene name: Rnf4

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 62%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided