3NL5
The Crystal Structure of Candida glabrata THI6, a Bifunctional Enzyme involved in Thiamin Biosyhthesis of Eukaryotes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
| A | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
| B | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004417 | molecular_function | hydroxyethylthiazole kinase activity |
| C | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0009228 | biological_process | thiamine biosynthetic process |
| C | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 541 |
| Chain | Residue |
| C | ASP340 |
| C | ACP999 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 541 |
| Chain | Residue |
| A | ASP340 |
| A | ACP799 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 541 |
| Chain | Residue |
| B | ASP340 |
| B | VAL342 |
| B | ACP899 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ACP A 799 |
| Chain | Residue |
| A | THR416 |
| A | GLY417 |
| A | GLU418 |
| A | ASP420 |
| A | ILE455 |
| A | MET458 |
| A | ALA463 |
| A | SER464 |
| A | GLY465 |
| A | CYS466 |
| A | LEU468 |
| A | TYR496 |
| A | LYS497 |
| A | MG541 |
| C | TZE542 |
| A | LYS367 |
| A | ASN369 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ACP B 899 |
| Chain | Residue |
| B | ASN369 |
| B | THR416 |
| B | GLY417 |
| B | GLU418 |
| B | ASP420 |
| B | ILE455 |
| B | MET458 |
| B | ALA463 |
| B | SER464 |
| B | GLY465 |
| B | CYS466 |
| B | LEU468 |
| B | LYS497 |
| B | MG541 |
| B | TZE542 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ACP C 999 |
| Chain | Residue |
| B | TZE543 |
| C | ASN369 |
| C | THR416 |
| C | GLY417 |
| C | ASP420 |
| C | ILE455 |
| C | MET458 |
| C | ALA463 |
| C | GLY465 |
| C | CYS466 |
| C | TYR496 |
| C | LYS497 |
| C | MG541 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TZE B 542 |
| Chain | Residue |
| A | PRO290 |
| A | MET292 |
| B | ASN272 |
| B | VAL274 |
| B | ALA463 |
| B | CYS466 |
| B | ACP899 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TZE C 542 |
| Chain | Residue |
| A | ASN272 |
| A | ARG350 |
| A | ACP799 |
| C | PRO290 |
| C | ILE291 |
| C | MET292 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TZE B 543 |
| Chain | Residue |
| B | PRO290 |
| B | ILE291 |
| B | MET292 |
| C | ASN272 |
| C | VAL274 |
| C | CYS466 |
| C | ACP999 |
