1RFT
Crystal structure of pyridoxal kinase complexed with AMP-PCP and pyridoxamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0042822 | biological_process | pyridoxal phosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | ACP401 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 404 |
| Chain | Residue |
| A | ASP113 |
| A | THR148 |
| A | THR186 |
| A | ACP401 |
| A | HOH417 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ACP A 401 |
| Chain | Residue |
| A | SER187 |
| A | MET223 |
| A | LYS225 |
| A | VAL226 |
| A | ALA228 |
| A | THR233 |
| A | GLY234 |
| A | PHE237 |
| A | LEU267 |
| A | ZN403 |
| A | K404 |
| A | HOH409 |
| A | TYR127 |
| A | ASN150 |
| A | THR186 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PXM A 402 |
| Chain | Residue |
| A | SER12 |
| A | VAL19 |
| A | HIS46 |
| A | THR47 |
| A | TYR84 |
| A | VAL231 |
| A | ASP235 |
| A | HOH433 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RFT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12235162","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LHR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RFT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RFU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12235162","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LHR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12235162","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LHR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| A | GLY234 | |
| A | THR233 | |
| A | GLY232 | |
| A | ASP235 |
