X-ray diffraction
1.61Å resolution

Crystal structure of the human UBR-box domain from UBR1 in complex with monomethylated arginine peptide.


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):
E3 ubiquitin-protein ligase UBR1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 76 amino acids
Theoretical weight: 8.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q8IWV7 (Residues: 98-168; Coverage: 4%)
Gene name: UBR1
Sequence domains: Putative zinc finger in N-recognin (UBR box)
NMM-ILE-PHE-SER peptide Chains: B, D
Molecule details ›
Chains: B, D
Length: 4 amino acids
Theoretical weight: 536 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 47.274Å b: 49.036Å c: 53.634Å
α: 90° β: 90° γ: 90°
R R work R free
0.15 0.149 0.18
Expression systems:
  • Escherichia coli
  • Not provided