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PDBe Entry: 1bya 
CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS
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HYDROLASE(O-GLYCOSYL)
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X-RAY DIFFRACTION
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Resolution: 2.2 Å, R-factor: 16.9%, Spacegroup: P 31 2 1
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31/07/1994, deposition: 25/01/1994, last revision: 24/02/2009
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Mikami, B.; Degano, M.; Hehre, E.J.; Sacchettini, J.C.
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Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis.
BIOCHEMISTRY vol:33, pag:7779-7787 (1994) [PubMed ID 8011643 ]
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HYDROLASE(O-GLYCOSYL)
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3.2.1.2 ExPASy BRENDA (A)
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Glycine max(soybean) 3847(A)
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Beta-amylase (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) P10538 (A)
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A
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| A |
BETA-AMYLASE |
Protein |
P10538 (AMYB_SOYBN)
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495 |
99% |
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| A |
SULFATE ION |
SO4
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