1B0I
ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
Summary for 1B0I
Entry DOI | 10.2210/pdb1b0i/pdb |
Descriptor | PROTEIN (ALPHA-AMYLASE), CALCIUM ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | alpha-amylase, alpha-1, 4-glucan-4-glucanohydrolase, beta-alpha-eight barrel, psychrophilic enzyme, hydrolase |
Biological source | Pseudoalteromonas haloplanktis |
Cellular location | Secreted : P29957 |
Total number of polymer chains | 1 |
Total formula weight | 49456.37 |
Authors | Aghajari, N.,Haser, R. (deposition date: 1998-11-10, release date: 1999-11-17, Last modification date: 2024-11-13) |
Primary citation | Aghajari, N.,Feller, G.,Gerday, C.,Haser, R. Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level. Structure, 6:1503-1506, 1998 Cited by PubMed Abstract: . Enzymes from psychrophilic (cold-adapted) microorganisms operate at temperatures close to 0 degreesC, where the activity of their mesophilic and thermophilic counterparts is drastically reduced. It has generally been assumed that thermophily is associated with rigid proteins, whereas psychrophilic enzymes have a tendency to be more flexible. PubMed: 9862804DOI: 10.1016/S0969-2126(98)00149-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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