› 3ny1

X-ray diffraction
2.08Å resolution

Structure of the ubr-box of the UBR1 ubiquitin ligase

Released:
DOI: 10.2210/pdb3ny1/pdb
PDB entry 3ny1 coloured by chain, front view.
PDB entry 3ny1 coloured by chain, side view.
PDB entry 3ny1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of substrate recognition and specificity in the N-end rule pathway.
Matta-Camacho E, Kozlov G, Li FF, Gehring K
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UBR1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 77 amino acids
Theoretical weight: 8.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8IWV7 (Residues: 97-168; Coverage: 4%)
Gene name: UBR1
Sequence domains: Putative zinc finger in N-recognin (UBR box)

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P21
Unit cell:
a: 29.702Å b: 49.262Å c: 43.831Å
α: 90° β: 100.51° γ: 90°
R-values:
R R work R free
0.2 0.194 0.248
Expression system: Escherichia coli BL21

Quick links

Citations

14 review citations

AAA+ proteases: ATP-fueled machines of protein destruction.
Sauer et al. (2011)
13 more

4 mentions without citation

Coupled Caspase and N-End Rule Ligase Activities Allow Recognition and Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic Development.
Weaver et al. (2017)
3 more