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*
Residue conservation analysis
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Biological unit*, dimer
(*as deduced by
)
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| PDB id: |
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1cqy
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| Name: |
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Hydrolase
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| Title: |
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Starch binding domain of bacillus cereus beta-amylase
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 Structure: |
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Beta-amylase. Chain: a. Fragment: starch-binding domain. Engineered: yes
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Source:
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Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biological unit:
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Dimer (from
)
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UniProt:
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| Seq: |
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| Struc: |
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| Seq: |
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| Struc: |
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| Seq: |
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546 a.a. |
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| Struc: |
99 a.a. |
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| Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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Reaction:
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Hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
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Resolution:
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1.95Å
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R-factor:
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0.181
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R-free:
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0.225
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Authors:
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H.J.Yoon,A.Hirata,M.Adachi,A.Sekine,S.Utsumi,B.Mikami
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Key ref:
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h.j.yoon
et al.
Structure of Separated Starch-Binding Domain of Bacillus cereus B-amylase.
To be Published,
xsi:nil="true" />.
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Date:
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12-Aug-99
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Release date:
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20-Aug-99
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Related entries:
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