1aqh
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ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
OverviewOverview
Alteromonas haloplanctis is a bacterium that flourishes in Antarctic, sea-water and it is considered as an extreme psychrophile. We have, determined the crystal structures of the alpha-amylase (AHA) secreted by, this bacterium, in its native state to 2.0 angstroms resolution as well as, in complex with Tris to 1.85 angstroms resolution. The structure of AHA, which is the first experimentally determined three-dimensional structure, of a psychrophilic enzyme, resembles those of other known alpha-amylases, of various origins with a surprisingly greatest similarity to mammalian, alpha-amylases. AHA contains a chloride ion which activates the hydrolytic, cleavage of substrate alpha-1,4-glycosidic bonds. The chloride binding, site is situated approximately 5 angstroms from the active site which ... [(full description)]
About this StructureAbout this Structure
1AQH is a [Single protein] structure of sequence from [Pseudoalteromonas haloplanktis] with CA and CL as [ligands]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Sites: AVE, CDE and CUM. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor., Aghajari N, Feller G, Gerday C, Haser R, Protein Sci. 1998 Mar;7(3):564-72. PMID:9541387
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