Function and Biology Details
Reaction catalysed:
Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-132780 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Actin, alpha skeletal muscle
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
UniProt:
Sequence domains: Actin
Structure domains:
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
UniProt:
- Canonical:
P68135 (Residues: 1-377; Coverage: 100%)
Sequence domains: Actin
Structure domains:
Deoxyribonuclease-1
Molecule details ›
Chain: D
Length: 260 amino acids
Theoretical weight: 29.09 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase
Length: 260 amino acids
Theoretical weight: 29.09 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P00639 (Residues: 23-282; Coverage: 100%)
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase
Gelsolin
Molecule details ›
Chain: G
Length: 125 amino acids
Theoretical weight: 14.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Gelsolin repeat
Structure domains: Severin
Length: 125 amino acids
Theoretical weight: 14.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P06396 (Residues: 52-176; Coverage: 17%)
Sequence domains: Gelsolin repeat
Structure domains: Severin
