Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-130741 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Type II toxin-antitoxin system RelE/ParE family toxin
Molecule details ›
Chains: A, C
Length: 90 amino acids
Theoretical weight: 10.9 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
Sequence domains: ParE toxin of type II toxin-antitoxin system, parDE
Structure domains: RelE-like
Length: 90 amino acids
Theoretical weight: 10.9 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
- Canonical:
O73966 (Residues: 1-90; Coverage: 100%)
Sequence domains: ParE toxin of type II toxin-antitoxin system, parDE
Structure domains: RelE-like
hypothetical protein PHS014
Molecule details ›
Chains: B, D
Length: 67 amino acids
Theoretical weight: 8 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
Sequence domains: Family of unknown function (DUF5646)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 67 amino acids
Theoretical weight: 8 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
- Canonical: O73967 (Residues: 1-67; Coverage: 100%)
Sequence domains: Family of unknown function (DUF5646)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL40B2
Spacegroup:
P21212
Expression system: Escherichia coli
