5ZQJ
Crystal structure of beta-xylosidase from Bacillus pumilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0045493 | biological_process | xylan catabolic process |
| B | 0000272 | biological_process | polysaccharide 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 | 0016787 | molecular_function | hydrolase 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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"A7LXU0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"A7LXU0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate","evidences":[{"source":"UniProtKB","id":"A7LXU0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
