Function and Biology Details
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Toxin RelE3 and Antitoxin RelB3 (preferred)
PDBe Complex ID:
PDB-CPX-143532 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Antitoxin RelB3
Molecule details ›
Chains: A, C
Length: 52 amino acids
Theoretical weight: 6.32 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
Sequence domains: RelB Antitoxin
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 52 amino acids
Theoretical weight: 6.32 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
- Canonical:
P0CL56 (Residues: 1-52; Coverage: 98%)
Sequence domains: RelB Antitoxin
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Toxin RelE3
Molecule details ›
Chains: B, D
Length: 88 amino acids
Theoretical weight: 10.52 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
Sequence domains: ParE toxin of type II toxin-antitoxin system, parDE
Structure domains: RelE-like
Length: 88 amino acids
Theoretical weight: 10.52 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
- Canonical: Q58503 (Residues: 1-88; Coverage: 100%)
Sequence domains: ParE toxin of type II toxin-antitoxin system, parDE
Structure domains: RelE-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
BESSY BEAMLINE 14.1
Spacegroup:
P21
Expression system: Escherichia coli
