2CEQ
Beta-glycosidase from Sulfolobus solfataricus in complex with glucoimidazole
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A1490 |
| Chain | Residue |
| A | GLY46 |
| A | SER49 |
| A | ALA434 |
| A | HOH2442 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT A1491 |
| Chain | Residue |
| A | ARG234 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B1490 |
| Chain | Residue |
| A | ASN113 |
| B | TYR2 |
| B | HIS410 |
| B | ASN414 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B1491 |
| Chain | Residue |
| B | THR323 |
| B | HIS342 |
| B | GIM1493 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B1492 |
| Chain | Residue |
| B | TRP455 |
| B | ARG463 |
| B | GLU464 |
| B | GLU474 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GIM A1492 |
| Chain | Residue |
| A | GLN18 |
| A | HIS150 |
| A | TRP151 |
| A | ASN205 |
| A | GLU206 |
| A | TYR322 |
| A | TRP361 |
| A | GLU387 |
| A | TRP425 |
| A | GLU432 |
| A | TRP433 |
| A | PHE441 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GIM B1493 |
| Chain | Residue |
| B | GLN18 |
| B | HIS150 |
| B | ASN205 |
| B | GLU206 |
| B | TYR322 |
| B | TRP361 |
| B | GLU387 |
| B | TRP425 |
| B | GLU432 |
| B | TRP433 |
| B | PHE441 |
| B | ACT1491 |
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 | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 | 8 |
| Details | Site: {"description":"Not N6-methylated"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| 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 | 4 |
| 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 | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU206 | |
| A | GLU387 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU206 | |
| B | GLU387 |
