1LHP
Crystal Structure of Pyridoxal Kinase from Sheep Brain
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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP 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 | 0016740 | molecular_function | transferase activity |
| B | 0042822 | biological_process | pyridoxal phosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 6 |
| 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 | 6 |
| 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 | 8 |
| 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 | 2 |
| 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 | 10 |
| 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 | 8 |
| 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 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| B | GLY234 | |
| B | THR233 | |
| B | GLY232 | |
| B | ASP235 |
