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1UG6

Structure of beta-glucosidase at atomic resolution from thermus thermophilus HB8

Replaces:  1UAH
Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 901
ChainResidue
AARG39
AGLY181
AARG183
AVAL330
APRO333
AASP378

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 902
ChainResidue
APHE395
AHOH924
AHOH1334
AHOH1420
AHIS178
ATRP312
AGLU392

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 903
ChainResidue
AGLN18
AHIS119
AASN163
AGLU164
AGLU338
ATRP385
AGLU392
ATRP393

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 904
ChainResidue
ALEU182
AASN184
AARG373
AGLY376
AVAL377
AASP378
AHOH933
AHOH945
AHOH1090
AHOH1266

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LYVTENGAA
ChainResidueDetails
ALEU334-ALA342

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtSAYQiEgA
ChainResidueDetails
APHE8-ALA22

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PDB entries from 2024-04-17

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