› 3o4g

X-ray diffraction
2.5Å resolution

Structure and Catalysis of Acylaminoacyl Peptidase

Released:
DOI: 10.2210/pdb3o4g/pdb
PDB entry 3o4g coloured by chain, front view.
PDB entry 3o4g coloured by chain, side view.
PDB entry 3o4g 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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 582 amino acids
Theoretical weight: 63.11 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

1 bound ligand:
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P1
Unit cell:
a: 71.212Å b: 97.016Å c: 109.494Å
α: 89.01° β: 109.2° γ: 100.21°
R-values:
R R work R free
0.218 0.215 0.262
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

5 mentions without citation

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