1UWI
CRYSTAL STRUCTURE OF MUTATED BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS, WORKING AT MODERATE TEMPERATURE
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 | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004565 | molecular_function | beta-galactosidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004565 | molecular_function | beta-galactosidase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008422 | molecular_function | beta-glucosidase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004565 | molecular_function | beta-galactosidase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008422 | molecular_function | beta-glucosidase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA |
| Chain | Residue | Details |
| A | MET383-ALA391 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FrFGwSqAGFQsEmG |
| Chain | Residue | Details |
| A | PHE8-GLY22 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU206 | |
| B | GLU206 | |
| C | GLU206 | |
| D | GLU206 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 |
| Chain | Residue | Details |
| A | GLU387 | |
| B | GLU387 | |
| C | GLU387 | |
| D | GLU387 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | SITE: Not N6-methylated |
| Chain | Residue | Details |
| A | LYS76 | |
| C | LYS102 | |
| C | LYS124 | |
| C | LYS138 | |
| D | LYS76 | |
| D | LYS102 | |
| D | LYS124 | |
| D | LYS138 | |
| A | LYS102 | |
| A | LYS124 | |
| A | LYS138 | |
| B | LYS76 | |
| B | LYS102 | |
| B | LYS124 | |
| B | LYS138 | |
| C | LYS76 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:14660666 |
| Chain | Residue | Details |
| A | LYS116 | |
| D | LYS116 | |
| D | LYS273 | |
| D | LYS311 | |
| A | LYS273 | |
| A | LYS311 | |
| B | LYS116 | |
| B | LYS273 | |
| B | LYS311 | |
| C | LYS116 | |
| C | LYS273 | |
| C | LYS311 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:14660666 |
| Chain | Residue | Details |
| A | LYS135 | |
| A | LYS332 | |
| B | LYS135 | |
| B | LYS332 | |
| C | LYS135 | |
| C | LYS332 | |
| D | LYS135 | |
| D | LYS332 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU206 | |
| A | ASN320 | |
| A | GLU387 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU206 | |
| B | ASN320 | |
| B | GLU387 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU206 | |
| C | ASN320 | |
| C | GLU387 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU206 | |
| D | ASN320 | |
| D | GLU387 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU206 | |
| A | GLU387 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU206 | |
| B | GLU387 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU206 | |
| C | GLU387 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU206 | |
| D | GLU387 |
