› 3o4i

X-ray diffraction
2.7Å resolution

Structure and Catalysis of Acylaminoacyl Peptidase

Released:
DOI: 10.2210/pdb3o4i/pdb
PDB entry 3o4i coloured by chain, front view.
PDB entry 3o4i coloured by chain, side view.
PDB entry 3o4i coloured by chain, top view.
Source organism: Aeropyrum pernix
Primary publication:
Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase.
Harmat V, Domokos K, Menyhárd DK, Palló A, Szeltner Z, Szamosi I, Beke-Somfai T, Náray-Szabó G, Polgár L
J Biol Chem 286 1987-98 (2011)
PMID: 21084296

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylamino-acid-releasing enzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 582 amino acids
Theoretical weight: 63.06 KDa
Source organism: Aeropyrum pernix
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YBQ2 (Residues: 1-582; Coverage: 100%)
Gene name: APE_1547.1
Sequence domains: Prolyl oligopeptidase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 6 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 103.63Å b: 209.89Å c: 205.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.252
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Gates of enzymes.
Gora et al. (2013)
2 more

1 mention without citation

Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase.
Harmat et al. (2011)