6q3t

X-ray diffraction
2.15Å resolution

Structure of Protease1 from Pyrococcus horikoshii at room temperature in ChipX microfluidic device

Released:

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
Molecule details ›
Chains: A, B, C
Length: 166 amino acids
Theoretical weight: 18.48 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
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P41212
Unit cell:
a: 125.56Å b: 125.56Å c: 133.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.185
Expression system: Escherichia coli