› 1k32

X-ray diffraction
2Å resolution

Crystal structure of the tricorn protease

Released:
DOI: 10.2210/pdb1k32/pdb
PDB entry 1k32 coloured by chain, front view.
PDB entry 1k32 coloured by chain, side view.
PDB entry 1k32 coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Crystal structure of the tricorn protease reveals a protein disassembly line.
Brandstetter H, Kim JS, Groll M, Huber R
Nature 414 466-70 (2001)
PMID: 11719810

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: 1045 amino acids
Theoretical weight: 118.68 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P96086 (Residues: 27-1071; Coverage: 98%)
Gene names: Ta1490, tri
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 95.86Å b: 245.998Å c: 159.04Å
α: 90° β: 105.296° γ: 90°
R-values:
R R work R free
0.245 0.245 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

The HtrA family of proteases: implications for protein composition and cell fate.
Clausen et al. (2002)
5 more

10 mentions without citation

Fast and anisotropic flexibility-rigidity index for protein flexibility and fluctuation analysis.
Opron et al. (2014)
9 more