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5GW7

Crystal structure of the glycosynthase mutant E727A of Escherichia coli GH63 glycosidase in complex with glucose and lactose

Replaces:  5CA4
Functional Information from GO Data
ChainGOidnamespacecontents
A0004555molecular_functionalpha,alpha-trehalase activity
A0005975biological_processcarbohydrate metabolic process
A0005991biological_processtrehalose metabolic process
A0005993biological_processtrehalose catabolic process
A0006974biological_processDNA damage response
A0008152biological_processmetabolic process
A0015926molecular_functionglucosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
A1901575biological_processorganic substance catabolic process
A1902687cellular_componentglucosidase complex
B0004555molecular_functionalpha,alpha-trehalase activity
B0005975biological_processcarbohydrate metabolic process
B0005991biological_processtrehalose metabolic process
B0005993biological_processtrehalose catabolic process
B0006974biological_processDNA damage response
B0008152biological_processmetabolic process
B0015926molecular_functionglucosidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
B1901575biological_processorganic substance catabolic process
B1902687cellular_componentglucosidase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP501
BASP501

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AALA727
BALA727

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP431
BVAL437
BGLU439
BGLU549
AASN433
AASN435
AVAL437
AGLU439
AGLU549
BASP431
BASN433
BASN435

218853

PDB entries from 2024-04-24

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