3WDP
Structural analysis of a beta-glucosidase mutant derived from a hyperthermophilic tetrameric structure
Functional Information from GO Data
Chain | GOid | namespace | contents |
P | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
P | 0005829 | cellular_component | cytosol |
P | 0005975 | biological_process | carbohydrate metabolic process |
P | 0008422 | molecular_function | beta-glucosidase activity |
P | 0016052 | biological_process | carbohydrate catabolic process |
P | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Q | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
Q | 0005829 | cellular_component | cytosol |
Q | 0005975 | biological_process | carbohydrate metabolic process |
Q | 0008422 | molecular_function | beta-glucosidase activity |
Q | 0016052 | biological_process | carbohydrate catabolic process |
Q | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
R | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
R | 0005829 | cellular_component | cytosol |
R | 0005975 | biological_process | carbohydrate metabolic process |
R | 0008422 | molecular_function | beta-glucosidase activity |
R | 0016052 | biological_process | carbohydrate catabolic process |
R | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
S | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
S | 0005829 | cellular_component | cytosol |
S | 0005975 | biological_process | carbohydrate metabolic process |
S | 0008422 | molecular_function | beta-glucosidase activity |
S | 0016052 | biological_process | carbohydrate catabolic process |
S | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL P 501 |
Chain | Residue |
P | GLN17 |
P | GOL504 |
P | HIS150 |
P | ASN206 |
P | GLU207 |
P | GLU372 |
P | TRP410 |
P | GLU417 |
P | TRP418 |
P | GOL503 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL P 502 |
Chain | Residue |
P | THR143 |
P | MET201 |
P | HOH928 |
P | HOH978 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL P 503 |
Chain | Residue |
P | PHE344 |
P | GLU417 |
P | GOL501 |
P | GOL504 |
P | HOH622 |
P | HOH903 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL P 504 |
Chain | Residue |
P | GLU207 |
P | ALA264 |
P | TYR307 |
P | GOL501 |
P | GOL503 |
P | HOH714 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 P 505 |
Chain | Residue |
P | PHE422 |
P | ARG425 |
P | HOH803 |
P | HOH936 |
P | HOH1013 |
Q | PHE468 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 P 506 |
Chain | Residue |
P | PHE91 |
P | LYS179 |
P | GLU183 |
P | LYS186 |
P | HOH687 |
P | HOH1021 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 P 507 |
Chain | Residue |
P | ASN213 |
P | LYS237 |
P | HOH621 |
P | HOH676 |
P | HOH844 |
P | HOH845 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 P 508 |
Chain | Residue |
P | ILE106 |
P | LYS298 |
P | HOH619 |
P | HOH734 |
P | HOH736 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL Q 501 |
Chain | Residue |
Q | GLN17 |
Q | HIS150 |
Q | ASN206 |
Q | GLU207 |
Q | GLU372 |
Q | TRP410 |
Q | GLU417 |
Q | TRP418 |
Q | GOL502 |
Q | GOL503 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL Q 502 |
Chain | Residue |
Q | PHE344 |
Q | GLU417 |
Q | GOL501 |
Q | GOL503 |
Q | HOH626 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL Q 503 |
Chain | Residue |
Q | GLU207 |
Q | VAL210 |
Q | ALA264 |
Q | TYR307 |
Q | GOL501 |
Q | GOL502 |
Q | HOH712 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 Q 504 |
Chain | Residue |
Q | ASP37 |
Q | GLU39 |
Q | ILE161 |
Q | LYS165 |
Q | HOH786 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 Q 505 |
Chain | Residue |
P | PHE468 |
Q | PHE422 |
Q | ARG425 |
Q | HOH797 |
Q | HOH798 |
Q | HOH1014 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 Q 506 |
Chain | Residue |
Q | PHE91 |
Q | LYS94 |
Q | LYS179 |
Q | GLU183 |
Q | LYS186 |
Q | HOH706 |
Q | HOH980 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 Q 507 |
Chain | Residue |
Q | ASN213 |
Q | LYS237 |
Q | HOH612 |
Q | HOH676 |
Q | HOH869 |
Q | HOH892 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL R 501 |
Chain | Residue |
R | GLU372 |
R | TRP410 |
R | GLU417 |
R | TRP418 |
R | GOL503 |
R | GLN17 |
R | HIS150 |
R | ASN206 |
R | GLU207 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL R 502 |
Chain | Residue |
Q | GLU128 |
Q | ARG131 |
R | ARG131 |
R | LYS132 |
R | SER135 |
R | HOH665 |
R | HOH874 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL R 503 |
Chain | Residue |
R | GLU207 |
R | VAL210 |
R | TYR307 |
R | GOL501 |
R | HOH869 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 R 504 |
Chain | Residue |
R | PHE91 |
R | LYS94 |
R | LYS179 |
R | VAL182 |
R | GLU183 |
R | LYS186 |
R | HOH685 |
R | HOH790 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 R 505 |
Chain | Residue |
R | TYR212 |
R | ASN213 |
R | GLU234 |
R | LYS237 |
R | HOH656 |
R | HOH892 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 R 506 |
Chain | Residue |
R | ASP269 |
R | PRO270 |
R | ARG309 |
R | HOH831 |
site_id | CC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL S 501 |
Chain | Residue |
S | GLN17 |
S | HIS150 |
S | ASN206 |
S | GLU207 |
S | GLU372 |
S | TRP410 |
S | GLU417 |
S | TRP418 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 S 502 |
Chain | Residue |
S | PHE91 |
S | LYS179 |
S | VAL182 |
S | GLU183 |
S | LYS186 |
S | HOH710 |
S | HOH829 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MIITENGMA |
Chain | Residue | Details |
P | MET368-ALA376 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmFGySwSGFQfEmG |
Chain | Residue | Details |
P | PHE7-GLY21 |