Function and Biology Details
Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136825 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 3
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 11.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Bromodomain extra-terminal - transcription regulation
Length: 96 amino acids
Theoretical weight: 11.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q15059 (Residues: 554-640; Coverage: 12%)
Sequence domains: Bromodomain extra-terminal - transcription regulation
Integrase
Molecule details ›
Chain: B
Length: 23 amino acids
Theoretical weight: 2.81 KDa
Source organism: Moloney murine leukemia virus isolate Shinnick
Expression system: Escherichia coli BL21(DE3)
UniProt:
Length: 23 amino acids
Theoretical weight: 2.81 KDa
Source organism: Moloney murine leukemia virus isolate Shinnick
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P03355 (Residues: 1716-1738; Coverage: 1%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
79%
Refinement method:
simulated annealing
Expression system: Escherichia coli BL21(DE3)
