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2ZQ0

Crystal structure of SusB complexed with acarbose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004339molecular_functionglucan 1,4-alpha-glucosidase activity
A0004558molecular_functionalpha-1,4-glucosidase activity
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0005983biological_processstarch catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0000272biological_processpolysaccharide catabolic process
B0004339molecular_functionglucan 1,4-alpha-glucosidase activity
B0004558molecular_functionalpha-1,4-glucosidase activity
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0005983biological_processstarch catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18981178","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18981178","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Substrate"}
ChainResidueDetails

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PDB entries from 2026-03-11

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