5M8B
Crystal structure of alpha-L-arabinofuranosidase from Lactobacillus brevis
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | GLU78 |
| A | HIS266 |
| A | HOH572 |
| A | HOH629 |
| A | HOH729 |
| A | HOH734 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue TRS A 402 |
| Chain | Residue |
| A | ASP141 |
| A | GLU202 |
| A | HIS266 |
| A | PGE403 |
| A | HOH509 |
| A | HOH574 |
| A | HOH732 |
| A | ASP17 |
| A | TRP75 |
| A | LEU140 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PGE A 403 |
| Chain | Residue |
| A | ASP17 |
| A | TYR37 |
| A | TRP75 |
| A | THR222 |
| A | ARG300 |
| A | TRS402 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PGE A 404 |
| Chain | Residue |
| A | LEU135 |
| A | GLN157 |
| A | ASP159 |
| A | TYR169 |
| A | PRO183 |
| A | HOH521 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue 1PE A 405 |
| Chain | Residue |
| A | THR24 |
| A | ASP25 |
| A | GLY26 |
| A | TYR27 |
| A | TYR27 |
| A | LYS46 |
| A | LYS46 |
| B | HOH508 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | GLU78 |
| B | HIS266 |
| B | HOH553 |
| B | HOH641 |
| B | HOH687 |
| B | HOH730 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue TRS B 402 |
| Chain | Residue |
| B | ASP17 |
| B | ASP141 |
| B | GLU202 |
| B | THR222 |
| B | TYR226 |
| B | HIS266 |
| B | ARG300 |
| B | HOH551 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue PG4 B 403 |
| Chain | Residue |
| B | GLY102 |
| B | PHE138 |
| B | ASN165 |
| B | ILE197 |
| B | PHE198 |
| B | HOH595 |
| B | HOH693 |
| B | HOH847 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue TRS B 404 |
| Chain | Residue |
| A | GLY66 |
| A | SER67 |
| B | LYS96 |
| B | PHE98 |
| B | TYR296 |
| B | HOH505 |
| B | HOH532 |
| B | HOH655 |
| B | HOH660 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue TRS B 405 |
| Chain | Residue |
| B | TYR19 |
| B | ILE20 |
| B | TYR21 |
| B | SER268 |
| B | PHE269 |
| B | HOH506 |
| B | HOH536 |
| B | HOH593 |
