› 1n6f

X-ray diffraction
2.7Å resolution

tricorn protease in complex with Z-Phe-diketo-Arg-Glu-Phe

Released:
DOI: 10.2210/pdb1n6f/pdb
PDB entry 1n6f coloured by chain, front view.
PDB entry 1n6f coloured by chain, side view.
PDB entry 1n6f coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum.
Kim JS, Groll M, Musiol HJ, Behrendt R, Kaiser M, Moroder L, Huber R, Brandstetter H
J Mol Biol 324 1041-50 (2002)
PMID: 12470958

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161195 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tricorn protease Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 1071 amino acids
Theoretical weight: 121.78 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P96086 (Residues: 1-1071; Coverage: 100%)
Gene names: Ta1490, tri
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DKT 6 x DKT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 95.67Å b: 244.55Å c: 158.32Å
α: 90° β: 104.59° γ: 90°
R-values:
R R work R free
0.247 0.247 0.28
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Molecular machines for protein degradation.
Groll et al. (2005)
1 more

1 mention without citation

Cyclodepsipeptides: Isolation from Endophytic Fungi of Sarcophyton ehrenbergi and Verification of Their Larvicidal Activity via In-Vitro and In-Silico Studies.
Singab et al. (2022)