1UWU
Structure of beta-glycosidase from Sulfolobus solfataricus in complex with D-glucohydroximo-1,5-lactam
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 1491 |
Chain | Residue |
A | HIS342 |
A | TRP361 |
A | HOH2270 |
A | HOH2272 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 1492 |
Chain | Residue |
A | HIS410 |
A | ARG411 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 1491 |
Chain | Residue |
B | HOH2278 |
B | HOH2438 |
B | TYR322 |
B | HIS342 |
B | GOX1490 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GOX A 1490 |
Chain | Residue |
A | GLN18 |
A | HIS150 |
A | ASN205 |
A | GLU206 |
A | TYR322 |
A | TRP361 |
A | GLU387 |
A | TRP425 |
A | GLU432 |
A | TRP433 |
A | PHE441 |
A | HOH2442 |
A | HOH2443 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GOX B 1490 |
Chain | Residue |
B | GLN18 |
B | HIS150 |
B | TRP151 |
B | ASN205 |
B | GLU206 |
B | TYR322 |
B | TRP361 |
B | GLU387 |
B | TRP425 |
B | GLU432 |
B | TRP433 |
B | PHE441 |
B | ACT1491 |
B | HOH2436 |
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 | ACT_SITE: Proton donor => ECO:0000255 |
Chain | Residue | Details |
A | GLU206 | |
B | GLU206 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 |
Chain | Residue | Details |
A | GLU387 | |
B | GLU387 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Not N6-methylated |
Chain | Residue | Details |
A | LYS76 | |
A | LYS102 | |
A | LYS124 | |
A | LYS138 | |
B | LYS76 | |
B | LYS102 | |
B | LYS124 | |
B | LYS138 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:14660666 |
Chain | Residue | Details |
A | LYS116 | |
A | LYS273 | |
A | LYS311 | |
B | LYS116 | |
B | LYS273 | |
B | LYS311 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:14660666 |
Chain | Residue | Details |
A | LYS135 | |
A | LYS332 | |
B | LYS135 | |
B | 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 | 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 |