8f1t

Electron Microscopy
12.1Å resolution

Structure of an 18mer DegP cage bound to the client protein hTRF1

Released:

Function and Biology Details

Reaction catalysed:
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero 54-mer (preferred)
PDBe Complex ID:
PDB-CPX-142919 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Periplasmic serine endoprotease DegP Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 348 amino acids
Theoretical weight: 36.38 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0V0 (Residues: 38-385; Coverage: 78%)
Gene names: JW0157, b0161, degP, htrA, ptd
Sequence domains:
Periplasmic serine endoprotease DegP Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 75 amino acids
Theoretical weight: 7.97 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0V0 (Residues: 400-474; Coverage: 17%)
Gene names: JW0157, b0161, degP, htrA, ptd
Sequence domains: PDZ domain
Telomeric repeat-binding factor 1 Chains: a, b, c
Molecule details ›
Chains: a, b, c
Length: 27 amino acids
Theoretical weight: 3.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54274 (Residues: 404-430; Coverage: 6%)
Gene names: PIN2, TERF1, TRBF1, TRF, TRF1
Sequence domains: Myb-like DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 12.1Å
Relevant EMDB volumes: EMD-28800
Expression system: Escherichia coli