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 | 0008378 | molecular_function | galactosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0008378 | molecular_function | galactosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase 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 | 0008378 | molecular_function | galactosyltransferase activity |
| C | 0016787 | molecular_function | hydrolase 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 | 0008378 | molecular_function | galactosyltransferase activity |
| D | 0016787 | molecular_function | hydrolase 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 | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Site: {"description":"Not N6-methylated"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-methyllysine; partial","evidences":[{"source":"PubMed","id":"14660666","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"14660666","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
