› 4hxe

X-ray diffraction
1.91Å resolution

Function and Biology Details

Reaction catalysed: 
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 622 amino acids
Theoretical weight: 73.34 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O58323 (Residues: 1-622; Coverage: 100%)
Gene name: PH0594
Sequence domains:
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand HEZ 6 x HEZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, EMBL/DESY, HAMBURG BEAMLINE X11, ESRF BEAMLINE BM14
Spacegroup: R32
Unit cell:
a: 183Å b: 183Å c: 144.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.172 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.
Brocca et al. (2016)
4 more

5 mentions without citation

A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization.
Menyhárd et al. (2013)
4 more