3IMH
CRYSTAL STRUCTURE OF GALACTOSE 1-EPIMERASE FROM Lactobacillus acidophilus NCFM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004034 | molecular_function | aldose 1-epimerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004034 | molecular_function | aldose 1-epimerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| 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 337 |
| Chain | Residue |
| A | HIS281 |
| A | HOH367 |
| A | HOH876 |
| B | HOH510 |
| B | HOH663 |
| B | HOH942 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 338 |
| Chain | Residue |
| B | HOH947 |
| B | HOH975 |
| A | HOH551 |
| B | HOH459 |
| B | HOH870 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 339 |
| Chain | Residue |
| A | GLY84 |
| A | HOH496 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 340 |
| Chain | Residue |
| A | PHE64 |
| A | HIS100 |
| A | HIS173 |
| A | TYR274 |
| A | HIS278 |
| A | GOL341 |
| A | HOH392 |
| A | HOH644 |
| A | HOH693 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 341 |
| Chain | Residue |
| A | GLY74 |
| A | ARG75 |
| A | ASP241 |
| A | GLU297 |
| A | GOL340 |
| A | HOH395 |
| A | HOH492 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 342 |
| Chain | Residue |
| A | ARG75 |
| A | ASP94 |
| A | GLU199 |
| A | ARG237 |
| A | HOH908 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 343 |
| Chain | Residue |
| A | LYS11 |
| A | TYR34 |
| A | SER59 |
| A | GLU61 |
| A | MET107 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 344 |
| Chain | Residue |
| A | ASN280 |
| A | GLY289 |
| A | GLN290 |
| A | HOH491 |
| B | LYS60 |
| B | HOH866 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 345 |
| Chain | Residue |
| A | ASP117 |
| A | HIS120 |
| A | ARG122 |
| A | GLU147 |
| A | HOH681 |
| A | HOH816 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 337 |
| Chain | Residue |
| B | HIS281 |
| B | HOH400 |
| B | HOH552 |
| B | HOH575 |
| B | HOH586 |
| B | HOH635 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 338 |
| Chain | Residue |
| B | PHE64 |
| B | HIS100 |
| B | HIS173 |
| B | TYR274 |
| B | HIS278 |
| B | GOL339 |
| B | HOH366 |
| B | HOH439 |
| B | HOH478 |
| B | HOH497 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 339 |
| Chain | Residue |
| B | GLY74 |
| B | ARG75 |
| B | ASP241 |
| B | GLU297 |
| B | GOL338 |
| B | HOH401 |
| B | HOH467 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 340 |
| Chain | Residue |
| B | ARG75 |
| B | ASP94 |
| B | GLU199 |
| B | ARG237 |
| B | HOH625 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 341 |
| Chain | Residue |
| B | HIS83 |
| B | GLY84 |
| B | HOH427 |
