Function and Biology Details
Reactions catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|- and the P1' position is occupied by Gly-|-
NTP + H(2)O = NDP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-566483 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase TRIM7
Molecule details ›
Chains: A, C
Length: 179 amino acids
Theoretical weight: 20.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 179 amino acids
Theoretical weight: 20.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9C029 (Residues: 342-511; Coverage: 33%)
Sequence domains:
NTPase
Molecule details ›
Chains: B, D
Length: 7 amino acids
Theoretical weight: 832 Da
Source organism: Murine norovirus 1
Expression system: Not provided
UniProt:
Length: 7 amino acids
Theoretical weight: 832 Da
Source organism: Murine norovirus 1
Expression system: Not provided
UniProt:
- Canonical: Q80J95 (Residues: 699-705; Coverage: 0%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
DIAMOND BEAMLINE I04
Spacegroup:
P21
Expression systems:
- Escherichia coli BL21(DE3)
- Not provided
