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
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178958 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase UBR5
Molecule details ›
Chains: A, C
Length: 65 amino acids
Theoretical weight: 7.1 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
Sequence domains: Poly-adenylate binding protein, unique domain
Structure domains: c-terminal domain of poly(a) binding protein
Length: 65 amino acids
Theoretical weight: 7.1 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q62671 (Residues: 2383-2442; Coverage: 2%)
Sequence domains: Poly-adenylate binding protein, unique domain
Structure domains: c-terminal domain of poly(a) binding protein
Polyadenylate-binding protein-interacting protein 1
Molecule details ›
Chains: B, D
Length: 22 amino acids
Theoretical weight: 2.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains: Ataxin-2 C-terminal region
Length: 22 amino acids
Theoretical weight: 2.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: Q9H074 (Residues: 123-144; Coverage: 5%)
Sequence domains: Ataxin-2 C-terminal region
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
CHESS BEAMLINE A1
Spacegroup:
P6422
Expression systems:
- Escherichia coli
- Not provided
