PDBe 3ny3

X-ray diffraction
1.6Å resolution

Structure of the ubr-box of UBR2 in complex with N-degron

Released:
Primary publication:
Structural basis of substrate recognition and specificity in the N-end rule pathway.
Nat. Struct. Mol. Biol. 17 1182-7 (2010)
PMID: 20835242

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-degron Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 523 Da
Source organism: Synthetic construct
Expression system: Not provided
E3 ubiquitin-protein ligase UBR2 Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 8.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8IWV8 (Residues: 98-167; Coverage: 4%)
Gene names: C6orf133, KIAA0349, UBR2
Sequence domains: Putative zinc finger in N-recognin (UBR box)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 29.123Å b: 36.94Å c: 29.824Å
α: 90° β: 109.6° γ: 90°
R-values:
R R work R free
0.192 0.19 0.21
Expression systems:
  • Not provided
  • Escherichia coli BL21