5ywr

X-ray diffraction
1.47Å resolution

Crystal Structure of RING E3 ligase ZNRF1 in complex with Ube2N (Ubc13)

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
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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158213 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 N Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61088 (Residues: 1-152; Coverage: 100%)
Gene names: BLU, UBE2N
Sequence domains: Ubiquitin-conjugating enzyme
E3 ubiquitin-protein ligase ZNRF1 Chain: B
Molecule details ›
Chain: B
Length: 89 amino acids
Theoretical weight: 10.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ND25 (Residues: 139-227; Coverage: 39%)
Gene names: NIN283, ZNRF1
Sequence domains: Ring finger domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RRCAT INDUS-2 BEAMLINE PX-BL21
Spacegroup: P212121
Unit cell:
a: 47.43Å b: 59.548Å c: 94.792Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.184
Expression system: Escherichia coli