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PDBe Entry: 2gjr view

Structure of bacillus halmapalus alpha-amylase without any substrate analogues
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.1 Å, R-factor: 20.189%, Free R-factor: 24.216%, Spacegroup: P 21 21 21
Released 05/09/2006, deposition: 31/03/2006, last revision: 24/02/2009
Authors Lyhne-Iversen, L.search; Hobley, T.J.search; Kaasgaard, S.G.search; Harris, P.search
Primary citation Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose.
ACTA CRYSTALLOGR.,SECT.Fsearch vol:62, pag:849-854 (2006) [PubMed ID 16946462 ]search
Keywords alpha-amylasesearch, bacillus halmapalussearch, HYDROLASEsearch
EC 3.2.1.98 ExPASy BRENDA search (A)
Organism Bacillus halmapalus 79882search(A)
UniProt Glucan 1,4-alpha-maltohexaosidase precursor (EC 3.2.1.98) (G6-amylase) (Maltohexaose-producing amylase) (Exo-maltohexaohydrolase) P19571search (A)
Solvent A
Related entries 1w9x, 2gjp
Polymers
Id Name Type UniProt Residues Observed
A alpha-amylase Protein P19571 (AMT6_BACS7)search
485 99%
Heterogens
Id Name Ligands
A CALCIUM ION CA search
A SODIUM ION NA search
A ACETATE ION ACT search
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