Function and Biology Details
Reactions 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
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159272 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-protein ligase E3A
Molecule details ›
Chains: A, B, C
Length: 358 amino acids
Theoretical weight: 41.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: HECT-domain (ubiquitin-transferase)
Structure domains:
Length: 358 amino acids
Theoretical weight: 41.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q05086 (Residues: 518-875; Coverage: 41%)
Sequence domains: HECT-domain (ubiquitin-transferase)
Structure domains:
Ubiquitin-conjugating enzyme E2 L3
Molecule details ›
Chain: D
Length: 154 amino acids
Theoretical weight: 17.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Length: 154 amino acids
Theoretical weight: 17.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P68036 (Residues: 1-154; Coverage: 100%)
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 5.0.2
Spacegroup:
P212121
Expression system: Escherichia coli
