3SCP
Crystal Structure of Rice BGlu1 E386A Mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004565 | molecular_function | beta-galactosidase activity |
| A | 0004567 | molecular_function | beta-mannosidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033907 | molecular_function | beta-D-fucosidase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042973 | molecular_function | glucan endo-1,3-beta-D-glucosidase activity |
| A | 0047668 | molecular_function | amygdalin beta-glucosidase activity |
| A | 0047701 | molecular_function | beta-L-arabinosidase activity |
| A | 0050224 | molecular_function | prunasin beta-glucosidase activity |
| A | 0080079 | molecular_function | cellobiose glucosidase activity |
| A | 0080083 | molecular_function | beta-gentiobiose beta-glucosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004565 | molecular_function | beta-galactosidase activity |
| B | 0004567 | molecular_function | beta-mannosidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0033907 | molecular_function | beta-D-fucosidase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042973 | molecular_function | glucan endo-1,3-beta-D-glucosidase activity |
| B | 0047668 | molecular_function | amygdalin beta-glucosidase activity |
| B | 0047701 | molecular_function | beta-L-arabinosidase activity |
| B | 0050224 | molecular_function | prunasin beta-glucosidase activity |
| B | 0080079 | molecular_function | cellobiose glucosidase activity |
| B | 0080083 | molecular_function | beta-gentiobiose beta-glucosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | ASP65 |
| A | HIS68 |
| B | ASP65 |
| B | HIS68 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | THR163 |
| A | ASN166 |
| A | ARG167 |
| A | HOH531 |
| A | HOH613 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1004 |
| Chain | Residue |
| B | THR163 |
| B | ASN166 |
| B | ARG167 |
| B | HOH587 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 1005 |
| Chain | Residue |
| A | GLY278 |
| A | HIS279 |
| A | TYR280 |
| A | GLN285 |
| A | LYS294 |
| A | PHE295 |
| A | ALA300 |
| A | HOH682 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES B 1006 |
| Chain | Residue |
| B | GLY278 |
| B | HIS279 |
| B | TYR280 |
| B | GLN285 |
| B | LYS294 |
| B | PHE295 |
| B | ALA300 |
| B | HOH509 |
| B | HOH776 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1007 |
| Chain | Residue |
| A | GLN29 |
| A | HIS130 |
| A | TRP433 |
| A | GLU440 |
| A | TRP441 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1008 |
| Chain | Residue |
| B | GLN29 |
| B | HIS130 |
| B | TYR315 |
| B | TRP433 |
| B | GLU440 |
| B | TRP441 |
| B | HOH622 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:25252199 |
| Chain | Residue | Details |
| A | GLU176 | |
| B | GLU176 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:25252199 |
| Chain | Residue | Details |
| A | ALA386 | |
| B | ALA386 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: 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 |
| Chain | Residue | Details |
| A | GLN29 | |
| A | GLU440 | |
| B | GLN29 | |
| B | GLU440 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: 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 |
| Chain | Residue | Details |
| A | HIS130 | |
| B | HIS130 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: 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 |
| Chain | Residue | Details |
| A | ASN175 | |
| B | ASN175 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: 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 |
| Chain | Residue | Details |
| A | TYR315 | |
| B | TYR315 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9 |
| Chain | Residue | Details |
| A | ALA386 | |
| B | ALA386 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305, ECO:0007744|PDB:3SCW |
| Chain | Residue | Details |
| A | TRP433 | |
| B | TRP433 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q1XH05 |
| Chain | Residue | Details |
| A | PHE449 | |
| B | PHE449 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | ASN252 | |
| A | ASN394 | |
| B | ASN252 | |
| B | ASN394 |
