› 2hu7

X-ray diffraction
2.01Å resolution

Binding of inhibitors by Acylaminoacyl peptidase

Released:
DOI: 10.2210/pdb2hu7/pdb
PDB entry 2hu7 coloured by chain, front view.
PDB entry 2hu7 coloured by chain, side view.
PDB entry 2hu7 coloured by chain, top view.
Source organism: Aeropyrum pernix
Primary publication:
The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity.
Kiss AL, Hornung B, Rádi K, Gengeliczki Z, Sztáray B, Juhász T, Szeltner Z, Harmat V, Polgár L
J Mol Biol 368 509-20 (2007)
PMID: 17350041

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 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: 63.11 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

3 bound ligands:
Ligand ACE 2 x ACE
Ligand PHE 2 x PHE
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 63.682Å b: 103.989Å c: 168.594Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.217
Expression system: Escherichia coli

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Citations

1 review citation

Dipeptidyl-peptidases: Key enzymes producing entry forms of extracellular proteins in asaccharolytic periodontopathic bacterium Porphyromonas gingivalis.
Nemoto et al. (2021)
17 other articles

2 mentions without citation

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