1TD2
Crystal Structure of the PdxY Protein from Escherichia coli
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 288 |
| Chain | Residue |
| B | GLY221 |
| B | VAL222 |
| B | GLY223 |
| B | ASP224 |
| B | PXL289 |
| B | HOH538 |
| B | HOH553 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PXL A 288 |
| Chain | Residue |
| A | THR45 |
| A | GLN46 |
| A | TYR83 |
| A | CYS122 |
| A | VAL220 |
| A | ASP224 |
| A | SER10 |
| A | HIS44 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PXL B 289 |
| Chain | Residue |
| B | SER10 |
| B | HIS44 |
| B | THR45 |
| B | TYR83 |
| B | CYS122 |
| B | VAL220 |
| B | ASP224 |
| B | SO4288 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15547280 |
| Chain | Residue | Details |
| A | SER10 | |
| A | THR45 | |
| A | ASP224 | |
| B | SER10 | |
| B | THR45 | |
| B | ASP224 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P40191 |
| Chain | Residue | Details |
| A | ASP112 | |
| B | ARG209 | |
| A | ALA144 | |
| A | GLU149 | |
| A | LYS182 | |
| A | ARG209 | |
| B | ASP112 | |
| B | ALA144 | |
| B | GLU149 | |
| B | LYS182 |
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 | 4 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| A | GLY221 | |
| A | ASP224 | |
| A | GLY223 | |
| A | VAL222 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1jxh |
| Chain | Residue | Details |
| B | GLY221 | |
| B | ASP224 | |
| B | GLY223 | |
| B | VAL222 |
