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Literature summary extracted from
- Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (2004), Structure, 12, 1481-1488.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.1 | Aeropyrum pernix | Q9YBQ2 | K1 | - |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | acylpeptide hydrolase/esterase | - |
Aeropyrum pernix |
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Release 2023.1 (January 2023)
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