› 1ve7

X-ray diffraction
2.7Å resolution

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate

Released:
DOI: 10.2210/pdb1ve7/pdb
PDB entry 1ve7 coloured by chain, front view.
PDB entry 1ve7 coloured by chain, side view.
PDB entry 1ve7 coloured by chain, top view.
Source organism: Aeropyrum pernix
Primary publication:
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1.
Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z
Structure 12 1481-8 (2004)
PMID: 15296741

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195455 (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

2 bound ligands:
Ligand 4NP 2 x 4NP
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 63.883Å b: 104.622Å c: 168.004Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.207 0.267
Expression system: Escherichia coli

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Citations

2 review citations

The metabolic serine hydrolases and their functions in mammalian physiology and disease.
Long et al. (2011)
1 more

5 mentions without citation

Carboxylic ester hydrolases from hyperthermophiles.
Levisson et al. (2009)
4 more