2DDW
Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene complexed with pyridoxal at 3.2 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008478 | molecular_function | pyridoxal kinase activity |
| A | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| A | 0016301 | molecular_function | kinase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036172 | biological_process | thiamine salvage |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008478 | molecular_function | pyridoxal kinase activity |
| B | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
| B | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| B | 0016301 | molecular_function | kinase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0036172 | biological_process | thiamine salvage |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PXL A 1003 |
| Chain | Residue |
| A | SER23 |
| A | PRO58 |
| A | HIS59 |
| A | ASP233 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PXL B 1005 |
| Chain | Residue |
| B | SER23 |
| B | PRO58 |
| B | HIS59 |
| B | ASP233 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16740960, ECO:0007744|PDB:2DDW |
| Chain | Residue | Details |
| A | SER23 | |
| A | HIS59 | |
| A | ASP233 | |
| B | SER23 | |
| B | HIS59 | |
| B | ASP233 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16740960, ECO:0007744|PDB:2DDO |
| Chain | Residue | Details |
| A | ASP125 | |
| B | THR231 | |
| A | THR157 | |
| A | THR195 | |
| A | HIS221 | |
| A | THR231 | |
| B | ASP125 | |
| B | THR157 | |
| B | THR195 | |
| B | HIS221 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16740960 |
| Chain | Residue | Details |
| A | TYR136 | |
| B | TYR136 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16740960 |
| Chain | Residue | Details |
| A | GLU162 | |
| B | GLU162 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| A | THR231 | |
| A | ASP233 | |
| A | GLY232 | |
| A | GLY230 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| B | THR231 | |
| B | ASP233 | |
| B | GLY232 | |
| B | GLY230 |
