3K1S
Crystal Structure of the PTS Cellobiose Specific Enzyme IIA from Bacillus anthracis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| E | 0016740 | molecular_function | transferase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| F | 0016740 | molecular_function | transferase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| G | 0016740 | molecular_function | transferase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| H | 0016740 | molecular_function | transferase activity |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| I | 0016740 | molecular_function | transferase activity |
| I | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 107 |
| Chain | Residue |
| A | ASP80 |
| A | HOH110 |
| A | HOH111 |
| B | ASP80 |
| B | HOH110 |
| C | ASP80 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 107 |
| Chain | Residue |
| E | ASP80 |
| E | HOH108 |
| F | ASP80 |
| D | ASP80 |
| D | HOH109 |
| D | HOH110 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 107 |
| Chain | Residue |
| G | ASP80 |
| G | HOH109 |
| H | ASP80 |
| I | ASP80 |
| I | HOH109 |
| I | HOH110 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA F 107 |
| Chain | Residue |
| F | GLU51 |
| F | PHE55 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA I 107 |
| Chain | Residue |
| H | TYR99 |
| I | GLU94 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 108 |
| Chain | Residue |
| A | GLU94 |
| B | LYS31 |
| B | TYR99 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA C 107 |
| Chain | Residue |
| B | GLU94 |
| C | LYS31 |
| C | TYR99 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA F 108 |
| Chain | Residue |
| D | LYS31 |
| D | TYR99 |
| F | GLU94 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA D 107 |
| Chain | Residue |
| D | GLU94 |
| E | LYS31 |
| E | TYR99 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA G 107 |
| Chain | Residue |
| G | GLU94 |
| I | LYS31 |
| I | TYR99 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA I 108 |
| Chain | Residue |
| D | GLN28 |
| I | GLU47 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 107 |
| Chain | Residue |
| A | TYR99 |
| C | GLU94 |
| C | LEU98 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA F 109 |
| Chain | Residue |
| E | GLU94 |
| E | ASP97 |
| F | LYS31 |
| F | TYR99 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA D 108 |
| Chain | Residue |
| B | PHE29 |
| B | HOH521 |
| D | GLU51 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA H 108 |
| Chain | Residue |
| F | GLN28 |
| F | GLN32 |
| H | GLU47 |
| H | ASN50 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 108 |
| Chain | Residue |
| A | GLU47 |
| A | ASN50 |
| E | GLN28 |
| E | GLN32 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 109 |
| Chain | Residue |
| A | GLU63 |
| A | LYS68 |
| A | THR69 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL H 109 |
| Chain | Residue |
| H | ARG20 |
| H | HIS81 |
| H | ASN84 |
| H | ALA85 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 108 |
| Chain | Residue |
| C | LYS44 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 109 |
| Chain | Residue |
| B | HIS53 |
| B | THR57 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| A | ASP80 | |
| A | HIS81 | |
| A | GLN79 | |
| A | HIS77 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| B | ASP80 | |
| B | HIS81 | |
| B | GLN79 | |
| B | HIS77 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| C | ASP80 | |
| C | HIS81 | |
| C | GLN79 | |
| C | HIS77 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| D | ASP80 | |
| D | HIS81 | |
| D | GLN79 | |
| D | HIS77 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| E | ASP80 | |
| E | HIS81 | |
| E | GLN79 | |
| E | HIS77 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| F | ASP80 | |
| F | HIS81 | |
| F | GLN79 | |
| F | HIS77 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| G | ASP80 | |
| G | HIS81 | |
| G | GLN79 | |
| G | HIS77 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| H | ASP80 | |
| H | HIS81 | |
| H | GLN79 | |
| H | HIS77 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e2a |
| Chain | Residue | Details |
| I | ASP80 | |
| I | HIS81 | |
| I | GLN79 | |
| I | HIS77 |
