1VI9
Crystal structure of pyridoxamine kinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042817 | biological_process | pyridoxal metabolic process |
| A | 0042819 | biological_process | vitamin B6 biosynthetic process |
| B | 0000166 | molecular_function | nucleotide 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 | 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 | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0042817 | biological_process | pyridoxal metabolic process |
| B | 0042819 | biological_process | vitamin B6 biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005524 | molecular_function | ATP 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 | 0016740 | molecular_function | transferase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0042816 | biological_process | vitamin B6 metabolic process |
| C | 0042817 | biological_process | pyridoxal metabolic process |
| C | 0042819 | biological_process | vitamin B6 biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005524 | molecular_function | ATP 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 | 0016740 | molecular_function | transferase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0042816 | biological_process | vitamin B6 metabolic process |
| D | 0042817 | biological_process | pyridoxal metabolic process |
| D | 0042819 | biological_process | vitamin B6 biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 298 |
| Chain | Residue |
| A | VAL220 |
| A | GLY221 |
| A | VAL222 |
| A | GLY223 |
| A | ASP224 |
| A | HOH530 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 298 |
| Chain | Residue |
| B | ASP224 |
| B | BME300 |
| B | HOH343 |
| B | HOH367 |
| B | HOH450 |
| B | HOH512 |
| B | HOH536 |
| B | GLY221 |
| B | VAL222 |
| B | GLY223 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 298 |
| Chain | Residue |
| C | GLY221 |
| C | VAL222 |
| C | GLY223 |
| C | ASP224 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 298 |
| Chain | Residue |
| D | GLY221 |
| D | VAL222 |
| D | GLY223 |
| D | ASP224 |
| D | BME300 |
| D | HOH337 |
| D | HOH520 |
| D | HOH523 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 300 |
| Chain | Residue |
| B | CYS122 |
| B | ASP224 |
| B | SO4298 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME D 300 |
| Chain | Residue |
| D | TYR83 |
| D | CYS122 |
| D | VAL220 |
| D | ASP224 |
| D | SO4298 |
| D | HOH357 |
| D | HOH523 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15547280","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P40191","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| A | GLY221 | |
| A | LYS182 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| B | GLY221 | |
| B | LYS182 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| C | GLY221 | |
| C | LYS182 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| D | GLY221 | |
| D | LYS182 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| A | GLY221 | |
| A | ASP224 | |
| A | GLY223 | |
| A | VAL222 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| B | GLY221 | |
| B | ASP224 | |
| B | GLY223 | |
| B | VAL222 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| C | GLY221 | |
| C | ASP224 | |
| C | GLY223 | |
| C | VAL222 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| D | GLY221 | |
| D | ASP224 | |
| D | GLY223 | |
| D | VAL222 |
