Function and Biology Details
Reaction catalysed:
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:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Ubiquitin and Ubiquitin-conjugating enzyme E2 K (preferred)
PDBe Complex ID:
PDB-CPX-143362 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 K
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 22.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 201 amino acids
Theoretical weight: 22.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P61086 (Residues: 1-200; Coverage: 100%)
Sequence domains:
Structure domains:
Ubiquitin
Molecule details ›
Chain: B
Length: 96 amino acids
Theoretical weight: 10.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 96 amino acids
Theoretical weight: 10.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P0CG48 (Residues: 608-683; Coverage: 11%)
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:
PAL/PLS BEAMLINE 4A
Spacegroup:
C2
Expression system: Escherichia coli
