5EFF
Crystal structure of an aromatic mutant (F4A) 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 | 3 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | ASN292 |
A | ARG351 |
A | ASP354 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue NA A 402 |
Chain | Residue |
A | SER18 |
A | ASP302 |
A | LEU305 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG B 401 |
Chain | Residue |
B | HOH502 |
B | HOH514 |
B | HOH528 |
B | ASN292 |
B | ARG351 |
B | ASP354 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue NA B 402 |
Chain | Residue |
B | SER18 |
B | ASP302 |
B | LEU305 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CL B 403 |
Chain | Residue |
B | GLY187 |
B | GLU188 |
B | GLU282 |
B | ARG283 |
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 |