8uq8

X-ray diffraction
2.34Å resolution

Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 2-residue linker

Released:

Function and Biology Details

Reactions 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
(1a) S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-[(E3-independent) ubiquitin-conjugating enzyme]-L-cysteine
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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-272305 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF168; Histone H2A type 1-B/E; Histone H2B type 2-E; Ubiquitin-conjugating enzyme E2 D3 Chains: A, a
Molecule details ›
Chains: A, a
Length: 437 amino acids
Theoretical weight: 48.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IYW5 (Residues: 1-94; Coverage: 17%)
  • Canonical: P61077 (Residues: 2-147; Coverage: 99%)
  • Canonical: Q16778 (Residues: 34-124; Coverage: 72%)
  • Canonical: P04908 (Residues: 13-106; Coverage: 72%)
Gene names: H2AC4, H2AC8, H2AFA, H2AFM, H2BC21, H2BFQ, HIST1H2AB, HIST1H2AE, HIST2H2BE, RNF168, UBC5C, UBCH5C, UBE2D3
Sequence domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P31
Unit cell:
a: 107.539Å b: 107.539Å c: 113.985Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.196 0.236
Expression system: Escherichia coli