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:
Ubiquitin and E3 ubiquitin-protein ligase RSP5 (preferred)
PDBe Complex ID:
PDB-CPX-143469 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RSP5
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 50.37 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 429 amino acids
Theoretical weight: 50.37 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P39940 (Residues: 384-809; Coverage: 53%)
Sequence domains:
Structure domains:
Ubiquitin
Molecule details ›
Chain: D
Length: 79 amino acids
Theoretical weight: 8.84 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 79 amino acids
Theoretical weight: 8.84 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: P0CG63 (Residues: 305-380; Coverage: 20%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
APS BEAMLINE 23-ID-D
Spacegroup:
C2
Expression system: Escherichia coli
