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Literature summary for 3.4.24.21 extracted from
- Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases (1993), Eur. J. Biochem., 214, 215-231.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| Astacus astacus | Astacus astacus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | requirement | Astacus astacus |  |
| Zn2+ | zinc metalloenzyme | Astacus astacus | |
| Zn2+ | zinc-binding consensus sequence | Astacus astacus | |
| Zn2+ | the catalytically active zinc is located at the bottom of the active-site cleft in the center of the molecule | Astacus astacus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
primary structure | Astacus astacus |
| additional information | - |
sequence alignment of enzymes of astacin family | Astacus astacus |
| additional information | - |
3-dimensional structure | Astacus astacus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Astacus astacus | - |
- |
- |
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