4RHH
Crystal structure of the catalytic mutant Xyn52B2-E335G, a GH52 Beta-D-xylosidase from Geobacillus stearothermophilus T6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009044 | molecular_function | xylan 1,4-beta-xylosidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009044 | molecular_function | xylan 1,4-beta-xylosidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0009044 | molecular_function | xylan 1,4-beta-xylosidase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0009044 | molecular_function | xylan 1,4-beta-xylosidase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 801 |
| Chain | Residue |
| A | ASP467 |
| A | ASN475 |
| A | VAL477 |
| A | HOH982 |
| A | HOH1011 |
| A | HOH1279 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS A 802 |
| Chain | Residue |
| A | HOH1193 |
| A | ASN364 |
| A | PHE368 |
| A | GLU371 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 803 |
| Chain | Residue |
| A | ASP345 |
| A | HIS396 |
| A | MET424 |
| A | THR493 |
| A | ASP495 |
| A | TRP632 |
| A | SER688 |
| A | TYR691 |
| A | ARG693 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 801 |
| Chain | Residue |
| B | ASP467 |
| B | ASN475 |
| B | VAL477 |
| B | HOH987 |
| B | HOH988 |
| B | HOH1016 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS B 802 |
| Chain | Residue |
| B | THR343 |
| B | ASP345 |
| B | HIS396 |
| B | MET424 |
| B | THR493 |
| B | ASP495 |
| B | TRP632 |
| B | SER688 |
| B | TYR691 |
| B | ARG693 |
| B | HOH1000 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 801 |
| Chain | Residue |
| C | ASP467 |
| C | ASN475 |
| C | VAL477 |
| C | HOH994 |
| C | HOH995 |
| C | HOH1030 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS C 802 |
| Chain | Residue |
| C | PHE368 |
| C | GLU371 |
| C | HOH1117 |
| C | HOH1118 |
| C | HOH1121 |
| C | HOH1256 |
| C | HOH1342 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TRS C 803 |
| Chain | Residue |
| C | THR343 |
| C | ASP345 |
| C | HIS396 |
| C | MET424 |
| C | THR493 |
| C | ASP495 |
| C | TRP632 |
| C | SER688 |
| C | TYR691 |
| C | ARG693 |
| C | HOH1012 |
| C | HOH1036 |
| C | HOH1354 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA C 804 |
| Chain | Residue |
| C | CYS420 |
| C | HOH1198 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 801 |
| Chain | Residue |
| D | ASP467 |
| D | ASN475 |
| D | VAL477 |
| D | HOH982 |
| D | HOH983 |
| D | HOH1048 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS D 802 |
| Chain | Residue |
| D | MET258 |
| D | LYS328 |
| D | PHE368 |
| D | GLU371 |
| D | HOH1147 |
| D | HOH1224 |
| D | HOH1328 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS D 803 |
| Chain | Residue |
| D | MET340 |
| D | ASP345 |
| D | HIS396 |
| D | THR493 |
| D | ASP495 |
| D | TRP632 |
| D | SER688 |
| D | TYR691 |
| D | ARG693 |
| D | HOH981 |
