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5IDI

Structure of beta glucosidase 1A from Thermotoga neapolitana, mutant E349A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0031217molecular_functionglucan 1,4-beta-glucosidase activity
A0102483molecular_functionscopolin beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0031217molecular_functionglucan 1,4-beta-glucosidase activity
B0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ACT A 501
ChainResidue
AGLN18
ATRP396
AGLU403
ATRP404
AHOH667
AHOH669

site_idAC2
Number of Residues5
Detailsbinding site for residue ACT A 502
ChainResidue
AHOH638
AHOH769
ASER294
AHIS296
ATRP322

site_idAC3
Number of Residues6
Detailsbinding site for residue ACT B 501
ChainResidue
BGLN18
BTRP396
BGLU403
BTRP404
BHOH665
BHOH666

Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS
ChainResidueDetails
APHE8-SER22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU164
BGLU164

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLY349
BGLY349

220113

PDB entries from 2024-05-22

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