1ESQ
CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S) WITH ATP AND THIAZOLE PHOSPHATE.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009228 | biological_process | thiamine biosynthetic process |
| C | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 340 |
| Chain | Residue |
| A | ATP300 |
| A | TZP320 |
| A | HOH575 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 345 |
| Chain | Residue |
| B | GLU126 |
| B | ATP305 |
| B | TZP325 |
| B | HOH497 |
| B | HOH505 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 350 |
| Chain | Residue |
| C | ATP310 |
| C | TZP330 |
| C | HOH480 |
| C | ARG121 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 355 |
| Chain | Residue |
| C | ATP310 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 360 |
| Chain | Residue |
| B | ATP305 |
| B | TZP325 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 365 |
| Chain | Residue |
| A | ATP300 |
| A | TZP320 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 370 |
| Chain | Residue |
| A | ASN26 |
| B | ASN26 |
| B | HOH501 |
| C | ASN26 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ATP A 300 |
| Chain | Residue |
| A | ARG121 |
| A | ASN123 |
| A | THR168 |
| A | GLY169 |
| A | GLU170 |
| A | ASP172 |
| A | HIS187 |
| A | LYS188 |
| A | LEU190 |
| A | THR191 |
| A | GLY197 |
| A | TZP320 |
| A | MG340 |
| A | MG365 |
| A | HOH567 |
| A | HOH568 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ATP B 305 |
| Chain | Residue |
| B | ARG121 |
| B | ASN123 |
| B | THR168 |
| B | GLY169 |
| B | GLU170 |
| B | ASP172 |
| B | ASN185 |
| B | HIS187 |
| B | LYS188 |
| B | LEU190 |
| B | GLY197 |
| B | TYR225 |
| B | TZP325 |
| B | MG345 |
| B | MG360 |
| B | HOH497 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP C 310 |
| Chain | Residue |
| C | ARG121 |
| C | ASN123 |
| C | THR168 |
| C | GLY169 |
| C | GLU170 |
| C | ASP172 |
| C | ASN185 |
| C | GLY186 |
| C | HIS187 |
| C | LEU190 |
| C | GLY197 |
| C | LEU200 |
| C | TYR225 |
| C | TZP330 |
| C | MG350 |
| C | MG355 |
| C | HOH441 |
| C | HOH480 |
| C | HOH565 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TZP A 320 |
| Chain | Residue |
| A | GLY67 |
| A | THR194 |
| A | GLY195 |
| A | GLY197 |
| A | SER198 |
| A | ATP300 |
| A | MG340 |
| A | MG365 |
| B | PRO43 |
| B | VAL44 |
| B | MET45 |
| site_id | BC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TZP B 325 |
| Chain | Residue |
| B | GLY67 |
| B | GLY195 |
| B | ALA196 |
| B | GLY197 |
| B | SER198 |
| B | ATP305 |
| B | MG345 |
| B | MG360 |
| B | HOH497 |
| B | HOH574 |
| C | PRO43 |
| C | VAL44 |
| C | MET45 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TZP C 330 |
| Chain | Residue |
| C | GLY67 |
| C | THR194 |
| C | GLY195 |
| C | GLY197 |
| C | SER198 |
| C | ATP310 |
| C | MG350 |
| C | HOH480 |
| A | PRO43 |
| A | VAL44 |
| A | MET45 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00228","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10891066","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
