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1E1F

Crystal structure of a Monocot (Maize ZMGlu1) beta-glucosidase in complex with p-Nitrophenyl-beta-D-thioglucoside

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009507cellular_componentchloroplast
A0009736biological_processcytokinin-activated signaling pathway
A0015923molecular_functionmannosidase activity
A0015925molecular_functiongalactosidase activity
A0015928molecular_functionfucosidase activity
A0016162molecular_functioncellulose 1,4-beta-cellobiosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0097599molecular_functionxylanase activity
A0102483molecular_functionscopolin beta-glucosidase activity
A0102726molecular_functionDIMBOA glucoside beta-D-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009507cellular_componentchloroplast
B0009736biological_processcytokinin-activated signaling pathway
B0015923molecular_functionmannosidase activity
B0015925molecular_functiongalactosidase activity
B0015928molecular_functionfucosidase activity
B0016162molecular_functioncellulose 1,4-beta-cellobiosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0097599molecular_functionxylanase activity
B0102483molecular_functionscopolin beta-glucosidase activity
B0102726molecular_functionDIMBOA glucoside beta-D-glucosidase activity
Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG
ChainResidueDetails
AILE402-GLY410

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA
ChainResidueDetails
APHE28-ALA42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q7XKV4
ChainResidueDetails
AGLU191
BGLU191

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q7XKV4
ChainResidueDetails
AGLU406
BGLU406

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49
ChainResidueDetails
AGLN38
BGLN38

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56
ChainResidueDetails
AHIS142
AASN190
ATYR333
ATYR473
BHIS142
BASN190
BTYR333
BTYR473

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9
ChainResidueDetails
AGLU406
BGLU406

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49
ChainResidueDetails
ATRP457
AGLU464
BTRP457
BGLU464

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU406
AASN331
AGLU191

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU406
BASN331
BGLU191

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU406
AGLU191

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU406
BGLU191

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU406
AASN331
AARG96
AGLU191
ATYR333
ATHR194

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU406
BASN331
BARG96
BGLU191
BTYR333
BTHR194

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PDB entries from 2024-09-11

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