5WKA
Crystal structure of a GH1 beta-glucosidase retrieved from microbial metagenome of Poraque Amazon lake
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0030245 | biological_process | cellulose catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0030245 | biological_process | cellulose catabolic process |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008422 | molecular_function | beta-glucosidase activity |
C | 0030245 | biological_process | cellulose catabolic process |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008422 | molecular_function | beta-glucosidase activity |
D | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | GLN16 |
A | GLU161 |
A | TYR292 |
A | GLU369 |
A | TRP416 |
A | GLU423 |
A | TRP424 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue PEG A 502 |
Chain | Residue |
A | GLY293 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | GLU161 |
B | TYR292 |
B | GLU369 |
B | TRP416 |
B | GLU423 |
B | TRP424 |
B | GLN16 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue PEG B 502 |
Chain | Residue |
B | CYS327 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
C | GLU161 |
C | TYR292 |
C | TRP342 |
C | GLU369 |
C | TRP416 |
C | GLU423 |
C | TRP424 |
C | PHE432 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | GLY425 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL D 501 |
Chain | Residue |
D | GLU161 |
D | TYR292 |
D | GLU369 |
D | TRP416 |
D | GLU423 |
D | TRP424 |
D | PHE432 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL D 502 |
Chain | Residue |
D | GLY39 |
D | GLY425 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue PEG D 503 |
Chain | Residue |
D | GLY293 |
D | TRP342 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LYITENGAA |
Chain | Residue | Details |
A | LEU365-ALA373 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FvWGtStAAYQiEgA |
Chain | Residue | Details |
A | PHE6-ALA20 |