5EFD
Crystal structure of a surface pocket creating mutant (W6A) of an alkali thermostable GH10 xylanase from Bacillus sp. NG-27
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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| 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 | 7 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASN292 |
| A | ARG351 |
| A | ASP354 |
| A | HOH521 |
| A | HOH540 |
| A | HOH625 |
| A | HOH662 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | LEU305 |
| A | HOH688 |
| A | HOH708 |
| A | SER18 |
| A | ASP302 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | PHE4 |
| A | ALA5 |
| A | ALA6 |
| A | LYS36 |
| A | TYR343 |
| A | HOH635 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | HIS90 |
| A | ASN91 |
| A | GLU149 |
| A | ARG162 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ALA75 |
| A | ARG76 |
| A | MET80 |
| A | ASP140 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | ARG162 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | ASN292 |
| B | ARG351 |
| B | ASP354 |
| B | HOH501 |
| B | HOH517 |
| B | HOH593 |
| B | HOH597 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 402 |
| Chain | Residue |
| B | SER18 |
| B | ASP302 |
| B | LEU305 |
| B | HOH690 |
| B | HOH700 |
| B | HOH705 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | PHE4 |
| B | ALA5 |
| B | ALA6 |
| B | ARG33 |
| B | TYR343 |
| B | HOH662 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | HIS230 |
| B | ILE231 |
| B | GLN232 |
| B | TRP267 |
| B | TRP319 |
| B | ARG323 |
| B | HOH541 |
| B | HOH574 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | ASP153 |
| B | VAL201 |
| B | THR202 |
| B | PRO203 |
| B | LYS204 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| A | ASN342 |
| B | ASP206 |
| B | TYR209 |
| B | ASN210 |
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 |
