3rtr

X-ray diffraction
3.21Å resolution

A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases

Released:

Function and Biology Details

Reactions 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
S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158746 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cullin-1 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 368 amino acids
Theoretical weight: 42.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13616 (Residues: 411-776; Coverage: 47%)
Gene name: CUL1
Sequence domains:
Structure domains:
E3 ubiquitin-protein ligase RBX1 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 106 amino acids
Theoretical weight: 12.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62877 (Residues: 5-108; Coverage: 96%)
Gene names: RBX1, RNF75, ROC1
Sequence domains: RING-H2 zinc finger domain
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 88.475Å b: 119.796Å c: 231.861Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.238 0.282
Expression system: Escherichia coli