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3D3I

Crystal structural of Escherichia coli K12 YgjK, a glucosidase belonging to glycoside hydrolase family 63

Replaces:  2DS3
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
A0016787molecular_functionhydrolase 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
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
B1902687cellular_componentglucosidase complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASP431
AASN433
AASN435
AGLU439
AGLU549

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 1001
ChainResidue
BGLU549
BASP431
BASN433
BASN435
BGLU439

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
APRO308
APHE315
ATRP321
AASP324
ALYS391
APHE742
ATRP744

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 2002
ChainResidue
ATRP321
AASP368
ALYS391
ATRP496

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 2001
ChainResidue
BPRO308
BPHE315
BTRP321
BASP324
BLYS391
BPHE742
BTRP744

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 2002
ChainResidue
BTRP321
BASP368
BLYS391

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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