2pie

X-ray diffraction
1.35Å resolution

Crystal structure of the FHA domain of RNF8 in complex with its optimal phosphopeptide

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 dimer (preferred)
PDBe Complex ID:
PDB-CPX-131199 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RNF8 Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 15.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O76064 (Residues: 13-146; Coverage: 28%)
Gene names: KIAA0646, RNF8
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
phosphopeptide Chain: F
Molecule details ›
Chain: F
Length: 7 amino acids
Theoretical weight: 1.02 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 34.632Å b: 76.865Å c: 120.744Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.198
Expression systems:
  • Escherichia coli
  • Not provided