7nj1

Electron Microscopy
2.9Å resolution

CryoEM structure of the human Separase-Securin complex

Released:

Function and Biology Details

Reaction catalysed:
All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132102 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Separin Chain: A
Molecule details ›
Chain: A
Length: 2160 amino acids
Theoretical weight: 237.61 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q14674 (Residues: 1-2120; Coverage: 100%)
Gene names: ESP1, ESPL1, KIAA0165
Sequence domains: Peptidase family C50
Securin Chain: B
Molecule details ›
Chain: B
Length: 202 amino acids
Theoretical weight: 22.05 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O95997 (Residues: 1-202; Coverage: 100%)
Gene names: EAP1, PTTG, PTTG1, TUTR1
Sequence domains: Securin sister-chromatid separation inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-12369
Expression system: Spodoptera frugiperda