1PX8
Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase
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 PROSITE/UniProt
| site_id | PS01027 |
| Number of Residues | 10 |
| Details | GLYCOSYL_HYDROL_F39 Glycosyl hydrolases family 39 active site. WpFEiWNEPN |
| Chain | Residue | Details |
| A | TRP153-ASN162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9761746","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| A | GLU160 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| B | GLU160 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| A | GLU277 | |
| A | ARG65 | |
| A | GLU160 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| B | GLU277 | |
| B | ARG65 | |
| B | GLU160 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| A | TRP153 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| B | TRP153 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| A | GLU277 | |
| A | GLU160 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pz3 |
| Chain | Residue | Details |
| B | GLU277 | |
| B | GLU160 |
