› 5c7m

X-ray diffraction
3.03Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-533890 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Itchy homolog Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 47.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96J02 (Residues: 524-899; Coverage: 42%)
Gene name: ITCH
Sequence domains: HECT-domain (ubiquitin-transferase)
Ubiquitin Chains: B, C
Molecule details ›
Chains: B, C
Length: 84 amino acids
Theoretical weight: 9.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 533-607; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P321
Unit cell:
a: 121.115Å b: 121.115Å c: 85.547Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.255 0.254 0.297
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

35 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
34 more

3 mentions without citation

Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants.
Gorelik et al. (2017)
2 more