› 2qr5

X-ray diffraction
2.2Å resolution

Aeropyrum pernix acylaminoacyl peptidase, H367A mutant

Released:
DOI: 10.2210/pdb2qr5/pdb
PDB entry 2qr5 coloured by chain, front view.
PDB entry 2qr5 coloured by chain, side view.
PDB entry 2qr5 coloured by chain, top view.
Source organism: Aeropyrum pernix
Primary publication:
Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase.
Kiss AL, Palló A, Náray-Szabó G, Harmat V, Polgár L
J Struct Biol 162 312-23 (2008)
PMID: 18325786

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: 63.04 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 102.27Å b: 105.04Å c: 114.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.222
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Mechanisms of intramolecular communication in a hyperthermophilic acylaminoacyl peptidase: a molecular dynamics investigation.
Papaleo et al. (2012)
8 more

1 mention without citation

Enhancing subtilisin thermostability through a modified normalized B-factor analysis and loop-grafting strategy.
Tang et al. (2019)