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1UA7

Crystal Structure Analysis of Alpha-Amylase from Bacillus Subtilis complexed with Acarbose

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005975biological_processcarbohydrate metabolic process
A0043169molecular_functioncation binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9514750","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9514750","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9514750","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9514750","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU208
AASP176

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU208
AHIS268
AASP269
AARG174
AASP176

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AHIS102
AGLU208
AASP269
AASP176

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP269
AGLU208
AASP176

249697

PDB entries from 2026-02-25

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