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1UWT

Structure of beta-glycosidase from Sulfolobus solfataricus in complex with D-galactohydroximo-1,5-lactam

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
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
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 1490
ChainResidue
AASN113
BHIS410
BARG411

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GTL A 1490
ChainResidue
AGLU387
ATRP425
AGLU432
ATRP433
APHE441
AGLN18
AHIS150
AASN205
AGLU206
ATYR322
ATRP361

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GTL B 1491
ChainResidue
BGLN18
BHIS150
BASN205
BGLU206
BTYR322
BTRP361
BGLU387
BTRP425
BGLU432
BTRP433
BPHE441
BHOH2483

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA
ChainResidueDetails
AMET383-ALA391

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FrFGwSqAGFQsEmG
ChainResidueDetails
APHE8-GLY22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU206
BGLU206

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU387
BGLU387

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Not N6-methylated
ChainResidueDetails
ALYS76
ALYS102
ALYS124
ALYS138
BLYS76
BLYS102
BLYS124
BLYS138

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:14660666
ChainResidueDetails
ALYS116
ALYS273
ALYS311
BLYS116
BLYS273
BLYS311

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:14660666
ChainResidueDetails
ALYS135
ALYS332
BLYS135
BLYS332

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PDB entries from 2024-03-27

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