1VI9
Crystal structure of pyridoxamine kinase
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 | 0008478 | molecular_function | pyridoxal kinase activity |
A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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: BINDING => ECO:0000269|PubMed:15547280 |
Chain | Residue | Details |
A | SER10 | |
D | SER10 | |
D | THR45 | |
D | ASP224 | |
A | THR45 | |
A | ASP224 | |
B | SER10 | |
B | THR45 | |
B | ASP224 | |
C | SER10 | |
C | THR45 | |
C | ASP224 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P40191 |
Chain | Residue | Details |
A | ASP112 | |
B | ARG209 | |
C | ASP112 | |
C | ALA144 | |
C | GLU149 | |
C | LYS182 | |
C | ARG209 | |
D | ASP112 | |
D | ALA144 | |
D | GLU149 | |
D | LYS182 | |
A | ALA144 | |
D | ARG209 | |
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 | 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 |