Function and Biology Details
Reaction catalysed:
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
R.HinP1I restriction endonuclease (preferred)
PDBe Complex ID:
PDB-CPX-177248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
R.HinP1I restriction endonuclease
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 28.79 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
Sequence domains: R.HinP1I restriction endonuclease
Structure domains: Trna Endonuclease; Chain: A, domain 1
Length: 247 amino acids
Theoretical weight: 28.79 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
- Canonical:
Q5I6E6 (Residues: 1-247; Coverage: 100%)
Sequence domains: R.HinP1I restriction endonuclease
Structure domains: Trna Endonuclease; 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:
NSLS BEAMLINE X8C
Spacegroup:
P6322
Expression system: Escherichia coli
