PDBe 2y4w

Solution NMR

Solution structure of human ubiquitin conjugating enzyme Rad6b

Released:
Source organism: Homo sapiens
Primary publication:
Symmetry and asymmetry of the RING-RING dimer of Rad18.
J. Mol. Biol. 410 424-35 (2011)
PMID: 21549715

Function and Biology Details

Reaction catalysed:
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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 B Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63146 (Residues: 1-152; Coverage: 100%)
Gene names: RAD6B, UBE2B
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 82%
Refinement method: CYANA
Chemical shifts: BMR17443  
Expression system: Escherichia coli BL21(DE3)