› 4hxf

X-ray diffraction
1.6Å resolution

Acylaminoacyl peptidase in complex with Z-Gly-Gly-Phe-chloromethyl ketone

Released:
DOI: 10.2210/pdb4hxf/pdb
PDB entry 4hxf coloured by chain, front view.
PDB entry 4hxf coloured by chain, side view.
PDB entry 4hxf coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization.
Menyhárd DK, Kiss-Szemán A, Tichy-Rács É, Hornung B, Rádi K, Szeltner Z, Domokos K, Szamosi I, Náray-Szabó G, Polgár L, Harmat V
J Biol Chem 288 17884-94 (2013)
PMID: 23632025

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
UniProt:
  • Canonical: O58323 (Residues: 1-622; Coverage: 100%)
Gene name: PH0594
Sequence domains:
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand Y3A 1 x Y3A
Ligand MG 5 x MG
Ligand HEZ 10 x HEZ
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R32
Unit cell:
a: 184.057Å b: 184.057Å c: 145.529Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.155 0.186
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

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

2 mentions without citation

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