5ZQJ
Crystal structure of beta-xylosidase from Bacillus pumilus
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 | 0009044 | molecular_function | xylan 1,4-beta-xylosidase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0045493 | biological_process | xylan catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0009044 | molecular_function | xylan 1,4-beta-xylosidase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue GOL A 601 |
Chain | Residue |
A | ASP14 |
A | PHE31 |
A | TRP73 |
A | ALA74 |
A | ASP127 |
A | ARG287 |
A | HOH822 |
A | HOH983 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 602 |
Chain | Residue |
A | GLN60 |
A | LEU61 |
A | ASP62 |
A | ASP90 |
A | TYR104 |
A | HOH902 |
A | SER59 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 603 |
Chain | Residue |
A | GLN279 |
A | ARG280 |
A | GLY281 |
A | TRP282 |
A | ASP496 |
A | HOH929 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue GOL B 601 |
Chain | Residue |
B | ASP14 |
B | PHE31 |
B | TRP73 |
B | ALA74 |
B | ASP127 |
B | THR206 |
B | ARG287 |
B | HOH785 |
B | HOH796 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL B 602 |
Chain | Residue |
B | GLN279 |
B | ARG280 |
B | GLY281 |
B | TRP282 |
B | ASP496 |
B | HOH830 |
B | HOH900 |
B | HOH975 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue GOL B 603 |
Chain | Residue |
B | SER59 |
B | GLN60 |
B | LEU61 |
B | ASP62 |
B | ASP90 |
B | TYR104 |
B | HOH807 |
B | HOH974 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A7LXU0 |
Chain | Residue | Details |
A | ASP14 | |
B | ASP14 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:A7LXU0 |
Chain | Residue | Details |
A | GLU186 | |
B | GLU186 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000250|UniProtKB:A7LXU0 |
Chain | Residue | Details |
A | ASP127 | |
B | ASP127 |