6XEP
Crystal structure of Thiamine-monophosphate kinase from Stenotrophomonas maltophilia K279a
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005524 | molecular_function | ATP binding |
A | 0009030 | molecular_function | thiamine-phosphate kinase activity |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 401 |
Chain | Residue |
A | ALA174 |
A | LEU175 |
A | ASN176 |
A | THR181 |
A | HOH673 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | ALA184 |
A | ASP185 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue NA A 403 |
Chain | Residue |
A | ILE22 |
A | HOH758 |
A | THR16 |
A | ARG19 |