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2WBG

Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-castanospermine

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
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
B0102483molecular_functionscopolin beta-glucosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
C0016052biological_processcarbohydrate catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0030245biological_processcellulose catabolic process
C0102483molecular_functionscopolin beta-glucosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
D0016052biological_processcarbohydrate catabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0030245biological_processcellulose catabolic process
D0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LGS A 1446
ChainResidue
AGLN20
ATRP398
AGLU405
ATRP406
AHOH2410
AHOH2411
AHIS121
AASN165
AGLU166
ATYR295
ASER296
AHIS298
ATRP324
AGLU351

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LGS B 1446
ChainResidue
BGLN20
BHIS121
BASN165
BGLU166
BTYR295
BHIS298
BTRP324
BGLU351
BTRP398
BGLU405
BTRP406
BHOH2190
BHOH2379

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE LGS C 1446
ChainResidue
CGLN20
CHIS121
CASN165
CGLU166
CTYR295
CSER296
CHIS298
CTRP324
CGLU351
CTRP398
CGLU405
CTRP406
CPHE414
CHOH2259
CHOH2519

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LGS D 1446
ChainResidue
DGLN20
DHIS121
DASN165
DGLU166
DTYR295
DHIS298
DTRP324
DGLU351
DTRP398
DGLU405
DTRP406
DPHE414
DHOH2454
DHOH2455

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT C 1447
ChainResidue
CTRP168
CASN246
CHOH2520
CHOH2521
CHOH2522

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VYITENGAA
ChainResidueDetails
AVAL347-ALA355

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS
ChainResidueDetails
APHE10-SER24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU166
BGLU166
CGLU166
DGLU166

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU351
BGLU351
CGLU351
DGLU351

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU166
AASN293
AGLU351

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU166
BASN293
BGLU351

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
CGLU166
CASN293
CGLU351

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
DGLU166
DASN293
DGLU351

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU166
AGLU351

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU166
BGLU351

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
CGLU166
CGLU351

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
DGLU166
DGLU351

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PDB entries from 2024-07-17

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