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1UOK

CRYSTAL STRUCTURE OF B. CEREUS OLIGO-1,6-GLUCOSIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0004574molecular_functionoligo-1,6-glucosidase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0009313biological_processoligosaccharide catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O06994","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 8370659, 9193006, 10331869
ChainResidueDetails
AASP199
AASP329
AGLU255

site_idMCSA1
Number of Residues5
DetailsM-CSA 285
ChainResidueDetails
AASP98electrostatic destabiliser, electrostatic stabiliser, repulsive charge-charge interaction, steric role
AASP199covalently attached, nucleofuge, nucleophile, polar interaction
AGLU255hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, repulsive charge-charge interaction
AHIS328electrostatic stabiliser, hydrogen bond donor
AASP329transition state stabiliser

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PDB entries from 2025-12-24

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