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1HXJ

CRYSTAL STRUCTURE OF THE MAIZE ZM-P60.1 BETA-GLUCOSIDASE

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_functionobsolete scopolin 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_functionobsolete scopolin 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
AILE397-GLY405

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA
ChainResidueDetails
APHE23-ALA37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q7XKV4
ChainResidueDetails
AGLU186
BGLU186

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q7XKV4
ChainResidueDetails
AGLU401
BGLU401

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
AGLN33
BGLN33

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56
ChainResidueDetails
AHIS137
AASN185
ATYR328
ATYR468
BHIS137
BASN185
BTYR328
BTYR468

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9
ChainResidueDetails
AGLU401
BGLU401

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
ATRP452
AGLU459
BTRP452
BGLU459

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU401
AGLU186
AASN326

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU401
BGLU186
BASN326

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU401
AGLU186

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU401
BGLU186

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU401
ATYR328
AASN326
AGLU186
ATHR189
AARG91

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU401
BTYR328
BASN326
BGLU186
BTHR189
BARG91

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PDB entries from 2024-10-30

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