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 | 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 | 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 |