› 1n6e

X-ray diffraction
2.6Å resolution

tricorn protease in complex with a tridecapeptide chloromethyl ketone derivative

Released:
DOI: 10.2210/pdb1n6e/pdb
PDB entry 1n6e coloured by chain, front view.
PDB entry 1n6e coloured by chain, side view.
PDB entry 1n6e coloured by chain, top view.
Source organisms:
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:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161197 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tricorn protease Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
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:
DQTQKAAAELTFF Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 14 amino acids
Theoretical weight: 1.5 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 95.47Å b: 245.1Å c: 157.89Å
α: 90° β: 105.19° γ: 90°
R-values:
R R work R free
0.254 0.254 0.288
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

2 review citations

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