5I3D
Sulfolobus solfataricus beta-glycosidase - E387Y 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 | 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 PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue PE8 A 501 |
Chain | Residue |
A | GLU112 |
A | ASN113 |
A | LYS116 |
A | ASP119 |
A | HOH749 |
A | HOH805 |
B | ILE413 |
B | ASN414 |
B | GLY416 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ACT A 502 |
Chain | Residue |
A | GLU206 |
A | TRP361 |
A | ACT503 |
A | HOH606 |
A | HOH667 |
A | HOH732 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT A 503 |
Chain | Residue |
A | PHE359 |
A | GLU432 |
A | TRP433 |
A | ACT502 |
A | HOH609 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue ACT A 504 |
Chain | Residue |
A | TRP84 |
A | PHE88 |
A | LEU92 |
A | LEU118 |
A | GLU182 |
A | ARG185 |
A | PHE186 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue ACT B 501 |
Chain | Residue |
B | GLU206 |
B | TRP361 |
B | ACT502 |
B | HOH608 |
B | HOH640 |
B | HOH641 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ACT B 502 |
Chain | Residue |
B | PHE359 |
B | GLU432 |
B | ACT501 |
B | HOH731 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue ACT B 503 |
Chain | Residue |
B | TRP84 |
B | PHE88 |
B | LEU92 |
B | GLU182 |
B | PHE186 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ACT B 504 |
Chain | Residue |
B | GLU279 |
B | GLU282 |
B | TRP287 |
B | LYS374 |
B | HOH719 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue ACT C 501 |
Chain | Residue |
C | GLU206 |
C | TRP361 |
C | ACT502 |
C | HOH638 |
C | HOH639 |
C | HOH651 |
C | HOH679 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ACT C 502 |
Chain | Residue |
C | PHE359 |
C | GLU432 |
C | ACT501 |
C | HOH612 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue ACT C 503 |
Chain | Residue |
C | TRP84 |
C | PHE88 |
C | LEU92 |
C | TRP156 |
C | GLU182 |
C | PHE186 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ACT D 501 |
Chain | Residue |
A | ARG463 |
D | GLU464 |
D | ASN468 |
D | ACT502 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue ACT D 502 |
Chain | Residue |
A | ARG463 |
D | GLU474 |
D | ACT501 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue ACT D 503 |
Chain | Residue |
D | GLU206 |
D | TYR322 |
D | TRP361 |
D | ACT504 |
D | HOH609 |
D | HOH647 |
D | HOH726 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue ACT D 504 |
Chain | Residue |
D | PHE359 |
D | GLU432 |
D | ACT503 |
D | HOH644 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue ACT D 505 |
Chain | Residue |
D | TRP84 |
D | PHE88 |
D | LEU92 |
D | LEU118 |
D | GLU182 |
D | PHE186 |
Functional Information from PROSITE/UniProt
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 | TYR387 | |
B | TYR387 | |
C | TYR387 | |
D | TYR387 |
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 |