2EXH
Structure of the family43 beta-Xylosidase 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 2001 |
| Chain | Residue |
| A | ASP333 |
| A | GLY362 |
| A | ASP528 |
| A | HOH2125 |
| A | HOH2139 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2002 |
| Chain | Residue |
| B | HOH2162 |
| B | HOH2308 |
| B | ASP333 |
| B | GLY362 |
| B | ASP528 |
| B | HOH2113 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 2003 |
| Chain | Residue |
| C | ASP333 |
| C | GLY362 |
| C | ASP528 |
| C | HOH2101 |
| C | HOH2113 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 2004 |
| Chain | Residue |
| D | ASP333 |
| D | GLY362 |
| D | ASP528 |
| D | HOH2138 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 2005 |
| Chain | Residue |
| A | VAL52 |
| A | ALA53 |
| A | ARG54 |
| A | HIS341 |
| A | HOH2316 |
| B | HIS389 |
| B | GLN468 |
| B | LEU535 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES B 2006 |
| Chain | Residue |
| B | LEU51 |
| B | VAL52 |
| B | ARG54 |
| B | ASN57 |
| B | ASP113 |
| B | GLY114 |
| B | HIS341 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES D 2007 |
| Chain | Residue |
| D | LEU51 |
| D | VAL52 |
| D | ALA53 |
| D | ARG54 |
| D | ASN57 |
| D | ASP113 |
| D | HIS341 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 2008 |
| Chain | Residue |
| A | SER60 |
| A | GLN61 |
| A | ASN63 |
| A | ASP91 |
| A | TYR105 |
| A | PRO119 |
| A | HOH2134 |
| A | HOH2425 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 2009 |
| Chain | Residue |
| B | SER60 |
| B | GLN61 |
| B | LEU62 |
| B | ASN63 |
| B | ASP91 |
| B | TYR105 |
| B | PRO119 |
| B | HOH2124 |
| B | HOH2467 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 2010 |
| Chain | Residue |
| C | SER60 |
| C | LEU62 |
| C | ASN63 |
| C | ASP91 |
| C | TYR105 |
| C | PRO119 |
| C | HOH2307 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 2011 |
| Chain | Residue |
| D | SER60 |
| D | GLN61 |
| D | LEU62 |
| D | ASN63 |
| D | ASP91 |
| D | TYR105 |
| D | PRO119 |
| D | HOH2033 |
