Function and Biology Details
Reactions catalysed:
ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine
S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186175 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NEDD8-activating enzyme E1 catalytic subunit
Molecule details ›
Chain: A
Length: 98 amino acids
Theoretical weight: 10.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: E2 binding domain
Structure domains: Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3
Length: 98 amino acids
Theoretical weight: 10.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8TBC4 (Residues: 368-463; Coverage: 21%)
Sequence domains: E2 binding domain
Structure domains: Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3
NEDD8-conjugating enzyme UBE2F
Molecule details ›
Chain: B
Length: 167 amino acids
Theoretical weight: 19.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Length: 167 amino acids
Theoretical weight: 19.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q969M7 (Residues: 21-185; Coverage: 89%)
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
