5XC0
Crystal structure of an aromatic mutant (W6A) of an alkali thermostable GH10 Xylanase from Bacillus sp. NG-27
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| A | 0045493 | biological_process | xylan catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| B | 0045493 | biological_process | xylan catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASN292 |
| A | ARG351 |
| A | ASP354 |
| A | HOH512 |
| A | HOH543 |
| A | HOH559 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | HOH616 |
| A | SER18 |
| A | ASP302 |
| A | LEU305 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | ASN292 |
| B | ARG351 |
| B | ASP354 |
| B | HOH502 |
| B | HOH503 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 402 |
| Chain | Residue |
| B | SER18 |
| B | ASP302 |
| B | LEU305 |
| B | HOH580 |
| B | HOH582 |
Functional Information from PROSITE/UniProt
| site_id | PS00591 |
| Number of Residues | 11 |
| Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLDNqVTELDV |
| Chain | Residue | Details |
| A | GLY252-VAL262 |
