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Literature summary for 3.4.19.1 extracted from

  • Bartlam, M.; Wang, G.; Yang, H.; Gao, R.; Zhao, X.; Xie, G.; Cao, S.; Feng, Y.; Rao, Z.
    Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (2004), Structure, 12, 1481-1488.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method. The best crystals were obtained from reservoir of 6% PEG4000, 50 mM/l NaAc (pH 4.6), 15 mM/l DTT, 0.2 mM/l EDTA Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2 K1
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Subunits

Subunits Comment Organism
dimer symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad Aeropyrum pernix

Synonyms

Synonyms Comment Organism
acylpeptide hydrolase/esterase
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Aeropyrum pernix