7qo8

X-ray diffraction
1.95Å resolution

Structure of Protease1 from Pyrococcus horikoshii in space group 19 with a hexamer in the asymmetric unit

Released:
Source organism: Pyrococcus horikoshii
Primary publication:
Medical contrast agents as promising tools for biomacromolecular SAXS experiments.
OpenAccess logo Acta Crystallogr D Struct Biol 78 1120-1130 (2022)
PMID: 36048152

Function and Biology Details

Reaction catalysed:
An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129858 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deglycase PH1704 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 166 amino acids
Theoretical weight: 18.65 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O59413 (Residues: 1-166; Coverage: 100%)
Gene name: PH1704
Sequence domains: DJ-1/PfpI family

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 115.741Å b: 123.636Å c: 129.223Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.204
Expression system: Escherichia coli