2I5B
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008478 | molecular_function | pyridoxal kinase activity |
| A | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| A | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008478 | molecular_function | pyridoxal kinase activity |
| B | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| B | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008478 | molecular_function | pyridoxal kinase activity |
| C | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| C | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
| C | 0009228 | biological_process | thiamine biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008478 | molecular_function | pyridoxal kinase activity |
| D | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| D | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
| D | 0009228 | biological_process | thiamine biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0008478 | molecular_function | pyridoxal kinase activity |
| E | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| E | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
| E | 0009228 | biological_process | thiamine biosynthetic process |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016310 | biological_process | phosphorylation |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 301 |
| Chain | Residue |
| A | ASN141 |
| A | ALA214 |
| A | GLY215 |
| A | LYS240 |
| A | ILE243 |
| A | ILE247 |
| A | THR178 |
| A | GLY180 |
| A | GLY181 |
| A | LYS182 |
| A | ALA188 |
| A | ASP190 |
| A | GLU204 |
| A | ILE206 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP C 401 |
| Chain | Residue |
| C | ASN141 |
| C | THR178 |
| C | GLY180 |
| C | GLY181 |
| C | LYS182 |
| C | ALA188 |
| C | ASP190 |
| C | GLU204 |
| C | ILE206 |
| C | ALA214 |
| C | GLY215 |
| C | LYS240 |
| C | ILE243 |
| C | ILE247 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP D 501 |
| Chain | Residue |
| D | ASN141 |
| D | THR178 |
| D | GLY180 |
| D | GLY181 |
| D | LYS182 |
| D | ALA188 |
| D | ASP190 |
| D | GLU204 |
| D | ILE206 |
| D | ALA214 |
| D | GLY215 |
| D | LYS240 |
| D | ILE243 |
| D | ILE247 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 601 |
| Chain | Residue |
| B | ASN141 |
| B | THR178 |
| B | GLY180 |
| B | GLY181 |
| B | LYS182 |
| B | ALA188 |
| B | ASP190 |
| B | GLU204 |
| B | ILE206 |
| B | ALA214 |
| B | GLY215 |
| B | LYS240 |
| B | ILE243 |
| B | ILE247 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP E 701 |
| Chain | Residue |
| E | ASN141 |
| E | THR178 |
| E | GLY180 |
| E | GLY181 |
| E | LYS182 |
| E | ALA188 |
| E | ASP190 |
| E | GLU204 |
| E | ILE206 |
| E | ALA214 |
| E | GLY215 |
| E | LYS240 |
| E | ILE243 |
| E | ILE247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN141 | |
| C | ILE206 | |
| C | GLY215 | |
| C | LYS240 | |
| D | ASN141 | |
| D | THR178 | |
| D | ASP190 | |
| D | ILE206 | |
| D | GLY215 | |
| D | LYS240 | |
| B | ASN141 | |
| A | THR178 | |
| B | THR178 | |
| B | ASP190 | |
| B | ILE206 | |
| B | GLY215 | |
| B | LYS240 | |
| E | ASN141 | |
| E | THR178 | |
| E | ASP190 | |
| E | ILE206 | |
| E | GLY215 | |
| A | ASP190 | |
| E | LYS240 | |
| A | ILE206 | |
| A | GLY215 | |
| A | LYS240 | |
| C | ASN141 | |
| C | THR178 | |
| C | ASP190 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU144 | |
| C | GLU144 | |
| D | GLU144 | |
| B | GLU144 | |
| E | GLU144 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| A | GLY215 | |
| A | CYS216 | |
| A | GLY213 | |
| A | ALA214 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| C | GLY215 | |
| C | CYS216 | |
| C | GLY213 | |
| C | ALA214 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| D | GLY215 | |
| D | CYS216 | |
| D | GLY213 | |
| D | ALA214 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| B | GLY215 | |
| B | CYS216 | |
| B | GLY213 | |
| B | ALA214 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| E | GLY215 | |
| E | CYS216 | |
| E | GLY213 | |
| E | ALA214 |
