4hxg

X-ray diffraction
2.7Å resolution

Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)

Released:

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-129709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 622 amino acids
Theoretical weight: 73.32 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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 183.31Å b: 183.8Å c: 275.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.241
Expression system: Escherichia coli BL21(DE3)