2EXI
Structure of the family43 beta-Xylosidase D15G mutant from geobacillus stearothermophilus
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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 3001 |
| Chain | Residue |
| A | ASP333 |
| A | GLY362 |
| A | ASP528 |
| A | HOH3086 |
| A | HOH3128 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 3002 |
| Chain | Residue |
| B | HOH3172 |
| B | HOH3504 |
| B | ASP333 |
| B | GLY362 |
| B | ASP528 |
| B | HOH3065 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 3003 |
| Chain | Residue |
| C | ASP333 |
| C | GLY362 |
| C | ASP528 |
| C | HOH3069 |
| C | HOH3137 |
| C | HOH3355 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 3004 |
| Chain | Residue |
| D | ASP333 |
| D | GLY362 |
| D | ASP528 |
| D | HOH3192 |
| D | HOH3482 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 3005 |
| Chain | Residue |
| A | VAL52 |
| A | ARG54 |
| A | HIS341 |
| B | HIS389 |
| B | GLN468 |
| B | LEU535 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES B 3006 |
| Chain | Residue |
| B | LEU51 |
| B | VAL52 |
| B | ALA53 |
| B | ARG54 |
| B | ASN57 |
| B | GLY114 |
| B | HIS341 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES D 3007 |
| Chain | Residue |
| D | LEU51 |
| D | VAL52 |
| D | ALA53 |
| D | ARG54 |
| D | ASP113 |
| D | HIS341 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 3008 |
| Chain | Residue |
| A | SER60 |
| A | GLN61 |
| A | ASN63 |
| A | ASP91 |
| A | TYR105 |
| A | PRO119 |
| A | HOH3213 |
| A | HOH3424 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 3009 |
| Chain | Residue |
| B | SER60 |
| B | GLN61 |
| B | LEU62 |
| B | ASN63 |
| B | ASP91 |
| B | TYR105 |
| B | HOH3232 |
| B | HOH3351 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 3010 |
| Chain | Residue |
| C | SER60 |
| C | GLN61 |
| C | ASN63 |
| C | ASP91 |
| C | TYR105 |
| C | PRO119 |
| C | HOH3274 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 3011 |
| Chain | Residue |
| D | SER60 |
| D | GLN61 |
| D | LEU62 |
| D | ASN63 |
| D | ASP91 |
| D | TYR105 |
| D | HOH3022 |
