› 5txw

X-ray diffraction
1.86Å resolution

Structure of Pfp1 protease from Thermococcus thioreducens: large cell H3 crystal form

Released:
DOI: 10.2210/pdb5txw/pdb
PDB entry 5txw coloured by chain, front view.
PDB entry 5txw coloured by chain, side view.
PDB entry 5txw coloured by chain, top view.
Source organism: Thermococcus thioreducens
Primary publication:
The structure of the Pfp1 protease from the hyperthermophilic archaeon Thermococcus thioreducens in two crystal forms.
Larson SB, McPherson A
Acta Crystallogr D Struct Biol 73 749-756 (2017)
PMID: 28876238

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DJ-1/PfpI domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 166 amino acids
Theoretical weight: 18.46 KDa
Source organism: Thermococcus thioreducens
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0Q2XKL6 (Residues: 1-166; Coverage: 100%)
Gene names: A3L14_09660, AMR53_10535, SAMN05216170_0004
Sequence domains: DJ-1/PfpI family
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
1 modified residue:
Ligand OCS 4 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: R3
Unit cell:
a: 152.85Å b: 152.85Å c: 82.541Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.13 0.127 0.173
Expression system: Escherichia coli

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Citations

1 review citation

Biotechnology of extremely thermophilic archaea.
Straub et al. (2018)