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
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
E3 ubiquitin-protein ligase UBR5 (preferred)
PDBe Complex ID:
PDB-CPX-131816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UBR5
Molecule details ›
Chain: A
Length: 61 amino acids
Theoretical weight: 6.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Poly-adenylate binding protein, unique domain
Structure domains: c-terminal domain of poly(a) binding protein
Length: 61 amino acids
Theoretical weight: 6.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O95071 (Residues: 2393-2453; Coverage: 2%)
Sequence domains: Poly-adenylate binding protein, unique domain
Structure domains: c-terminal domain of poly(a) binding protein
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P212121
Expression system: Escherichia coli BL21(DE3)
