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7VT9

CRYSTAL STRUCTURE AT 3.4 ANGSTROMS RESOLUTION OF Maltodextrin glucosidase, MalZ, FROM Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000023biological_processmaltose metabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004558molecular_functionalpha-1,4-glucosidase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030980biological_processalpha-glucan catabolic process
A0032450molecular_functionmaltose alpha-glucosidase activity
A0042803molecular_functionprotein homodimerization activity
B0000023biological_processmaltose metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004558molecular_functionalpha-1,4-glucosidase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030980biological_processalpha-glucan catabolic process
B0032450molecular_functionmaltose alpha-glucosidase activity
B0042803molecular_functionprotein homodimerization activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP336
BASP336

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU373
BGLU373

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP448
BASP448

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PDB entries from 2024-07-10

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