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
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
E3 ubiquitin-protein ligase UBR5 and Ubiquitin (preferred)
PDBe Complex ID:
PDB-CPX-131817 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin
Molecule details ›
Chains: A, C, E, G
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P0CH28 (Residues: 609-684; Coverage: 11%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
E3 ubiquitin-protein ligase UBR5
Molecule details ›
Chains: B, D, F, H
Length: 53 amino acids
Theoretical weight: 5.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: E3 ubiquitin ligase EDD
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Length: 53 amino acids
Theoretical weight: 5.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: O95071 (Residues: 180-230; Coverage: 2%)
Sequence domains: E3 ubiquitin ligase EDD
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
NSLS BEAMLINE X29A
Spacegroup:
P212121
Expression system: Escherichia coli BL21
