3MBH
Crystal structure of a putative phosphomethylpyrimidine kinase (BT_4458) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 2.00 A resolution (orthorhombic form with pyridoxal)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0008478 | molecular_function | pyridoxal kinase activity |
| A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008478 | molecular_function | pyridoxal kinase activity |
| B | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008478 | molecular_function | pyridoxal kinase activity |
| C | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| C | 0042816 | biological_process | vitamin B6 metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008478 | molecular_function | pyridoxal kinase activity |
| D | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
| D | 0042816 | biological_process | vitamin B6 metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0008478 | molecular_function | pyridoxal kinase activity |
| E | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016310 | biological_process | phosphorylation |
| E | 0042816 | biological_process | vitamin B6 metabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0008478 | molecular_function | pyridoxal kinase activity |
| F | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016310 | biological_process | phosphorylation |
| F | 0042816 | biological_process | vitamin B6 metabolic process |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXL A 400 |
| Chain | Residue |
| A | ASP14 |
| A | ASP224 |
| A | HOH303 |
| A | SER16 |
| A | LEU45 |
| A | HIS48 |
| A | THR49 |
| A | GLN50 |
| A | TYR84 |
| A | VAL113 |
| A | TYR121 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 291 |
| Chain | Residue |
| A | ASN201 |
| A | TRP208 |
| A | HOH331 |
| A | HOH354 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PXL B 400 |
| Chain | Residue |
| B | ASP14 |
| B | HIS48 |
| B | THR49 |
| B | GLN50 |
| B | TYR84 |
| B | VAL113 |
| B | TYR121 |
| B | ASP224 |
| B | HOH320 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXL C 400 |
| Chain | Residue |
| C | ASP14 |
| C | SER16 |
| C | LEU45 |
| C | HIS48 |
| C | THR49 |
| C | GLN50 |
| C | TYR84 |
| C | TYR121 |
| C | ASP224 |
| C | HOH356 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 291 |
| Chain | Residue |
| B | HOH292 |
| C | ASN201 |
| C | TRP208 |
| C | HOH323 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXL D 400 |
| Chain | Residue |
| D | ASP14 |
| D | SER16 |
| D | LEU45 |
| D | HIS48 |
| D | THR49 |
| D | GLN50 |
| D | TYR84 |
| D | VAL113 |
| D | TYR121 |
| D | ASP224 |
| D | HOH347 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXL E 400 |
| Chain | Residue |
| E | ASP14 |
| E | SER16 |
| E | LEU45 |
| E | HIS48 |
| E | THR49 |
| E | GLN50 |
| E | TYR84 |
| E | VAL113 |
| E | TYR121 |
| E | ASP224 |
| E | HOH319 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL E 291 |
| Chain | Residue |
| E | ASN201 |
| E | TRP208 |
| E | HOH297 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXL F 400 |
| Chain | Residue |
| F | ASP14 |
| F | SER16 |
| F | VAL21 |
| F | LEU45 |
| F | HIS48 |
| F | THR49 |
| F | GLN50 |
| F | TYR84 |
| F | VAL113 |
| F | ASP224 |
| F | HOH427 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL F 291 |
| Chain | Residue |
| F | ASN201 |
| F | TRP208 |
