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3W7W

Crystal structure of E. coli YgjK E727A complexed with 2-O-alpha-D-glucopyranosyl-alpha-D-galactopyranose

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
A0009313biological_processoligosaccharide catabolic process
A0015926molecular_functionglucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
A1902687cellular_componentglucosidase complex
B0004555molecular_functionalpha,alpha-trehalase activity
B0005975biological_processcarbohydrate metabolic process
B0005991biological_processtrehalose metabolic process
B0005993biological_processtrehalose catabolic process
B0006974biological_processDNA damage response
B0009313biological_processoligosaccharide catabolic process
B0015926molecular_functionglucosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
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

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PDB entries from 2024-10-30

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