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3SCR

Crystal Structure of Rice BGlu1 E386S Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0004567molecular_functionbeta-mannosidase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033907molecular_functionbeta-D-fucosidase activity
A0042803molecular_functionprotein homodimerization activity
A0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
A0047668molecular_functionamygdalin beta-glucosidase activity
A0047701molecular_functionbeta-L-arabinosidase activity
A0050224molecular_functionprunasin beta-glucosidase activity
A0080079molecular_functioncellobiose glucosidase activity
A0080083molecular_functionbeta-gentiobiose beta-glucosidase activity
A0102483molecular_functionscopolin beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0004567molecular_functionbeta-mannosidase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033907molecular_functionbeta-D-fucosidase activity
B0042803molecular_functionprotein homodimerization activity
B0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
B0047668molecular_functionamygdalin beta-glucosidase activity
B0047701molecular_functionbeta-L-arabinosidase activity
B0050224molecular_functionprunasin beta-glucosidase activity
B0080079molecular_functioncellobiose glucosidase activity
B0080083molecular_functionbeta-gentiobiose beta-glucosidase activity
B0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AASP65
AHIS68
BASP65
BHIS68

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
ATHR163
AASN166
AARG167
AHOH543
AHOH547

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 1005
ChainResidue
AGLY278
AHIS279
ATYR280
AGLN285
ALYS294
APHE295
AALA300
AHOH688
AHOH785

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1007
ChainResidue
AGLN29
AHIS130
ATRP433
AGLU440
ATRP441
AHOH788

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1004
ChainResidue
BTHR163
BASN166
BARG167
BHOH554
BHOH675

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MES B 1006
ChainResidue
ALEU395
BGLY278
BHIS279
BTYR280
BGLN285
BLYS294
BPHE295
BALA300
BHOH762
BHOH824

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1008
ChainResidue
BGLN29
BHIS130
BTRP433
BGLU440
BTRP441
BHOH867

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:25252199
ChainResidueDetails
AGLU176
BGLU176

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:25252199
ChainResidueDetails
ASER386
BSER386

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:18308333, ECO:0000305|PubMed:20884352, ECO:0000305|PubMed:25252199, ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT, ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK
ChainResidueDetails
AGLN29
AGLU440
BGLN29
BGLU440

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:20884352, ECO:0000305|PubMed:25252199, ECO:0007744|PDB:3AHT, ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK
ChainResidueDetails
AHIS130
BHIS130

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18308333, ECO:0000305|PubMed:20884352, ECO:0000305|PubMed:25252199, ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK
ChainResidueDetails
AASN175
BASN175

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18308333, ECO:0000305|PubMed:20884352, ECO:0000305|PubMed:25252199, ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK
ChainResidueDetails
ATYR315
BTYR315

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9
ChainResidueDetails
ASER386
BSER386

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305, ECO:0007744|PDB:3SCW
ChainResidueDetails
ATRP433
BTRP433

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q1XH05
ChainResidueDetails
APHE449
BPHE449

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN252
AASN394
BASN252
BASN394

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PDB entries from 2024-07-17

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