3GFB
L-Threonine Dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006566 | biological_process | threonine metabolic process |
| A | 0006567 | biological_process | threonine catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0019518 | biological_process | L-threonine catabolic process to glycine |
| A | 0030554 | molecular_function | adenyl nucleotide binding |
| A | 0043168 | molecular_function | anion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051262 | biological_process | protein tetramerization |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006566 | biological_process | threonine metabolic process |
| B | 0006567 | biological_process | threonine catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0019518 | biological_process | L-threonine catabolic process to glycine |
| B | 0030554 | molecular_function | adenyl nucleotide binding |
| B | 0043168 | molecular_function | anion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051262 | biological_process | protein tetramerization |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006566 | biological_process | threonine metabolic process |
| C | 0006567 | biological_process | threonine catabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0019518 | biological_process | L-threonine catabolic process to glycine |
| C | 0030554 | molecular_function | adenyl nucleotide binding |
| C | 0043168 | molecular_function | anion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051262 | biological_process | protein tetramerization |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0070403 | molecular_function | NAD+ binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006566 | biological_process | threonine metabolic process |
| D | 0006567 | biological_process | threonine catabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016597 | molecular_function | amino acid binding |
| D | 0019518 | biological_process | L-threonine catabolic process to glycine |
| D | 0030554 | molecular_function | adenyl nucleotide binding |
| D | 0043168 | molecular_function | anion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051262 | biological_process | protein tetramerization |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A 500 |
| Chain | Residue |
| A | GLY175 |
| A | SER244 |
| A | ALA246 |
| A | ALA249 |
| A | LEU266 |
| A | GLY267 |
| A | LEU268 |
| A | ILE291 |
| A | THR292 |
| A | HOH404 |
| A | HOH421 |
| A | GLY177 |
| A | HOH422 |
| A | HOH425 |
| A | HOH449 |
| A | HOH562 |
| B | ILE282 |
| A | PRO178 |
| A | LEU179 |
| A | SER198 |
| A | GLU199 |
| A | PRO200 |
| A | ARG204 |
| A | PHE243 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| A | ILE282 |
| B | GLY177 |
| B | PRO178 |
| B | LEU179 |
| B | SER198 |
| B | GLU199 |
| B | PRO200 |
| B | ARG204 |
| B | PRO219 |
| B | PHE243 |
| B | SER244 |
| B | ALA246 |
| B | LEU266 |
| B | LEU268 |
| B | ILE291 |
| B | THR292 |
| B | HOH412 |
| B | HOH414 |
| B | HOH441 |
| B | HOH446 |
| B | HOH447 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 351 |
| Chain | Residue |
| B | LEU162 |
| B | GLY164 |
| B | PRO165 |
| C | PRO165 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 352 |
| Chain | Residue |
| B | TYR147 |
| B | GLY310 |
| B | LEU312 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 353 |
| Chain | Residue |
| B | ASP223 |
| B | VAL225 |
| B | GLN252 |
| B | LYS255 |
| B | HOH527 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 354 |
| Chain | Residue |
| B | PRO247 |
| B | GLU251 |
| B | ARG271 |
| B | VAL273 |
| B | THR274 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 355 |
| Chain | Residue |
| B | ARG271 |
| B | GLU272 |
| C | PRO270 |
| C | ARG271 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD C 502 |
| Chain | Residue |
| C | GLY175 |
| C | GLY177 |
| C | PRO178 |
| C | LEU179 |
| C | GLY180 |
| C | SER198 |
| C | GLU199 |
| C | PRO200 |
| C | ARG204 |
| C | PHE243 |
| C | SER244 |
| C | ALA246 |
| C | ALA249 |
| C | LEU266 |
| C | GLY267 |
| C | LEU268 |
| C | ILE291 |
| C | THR292 |
| C | HOH411 |
| C | HOH451 |
| C | HOH453 |
| C | HOH455 |
| C | HOH456 |
| C | HOH457 |
| C | HOH615 |
| D | ILE282 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 351 |
| Chain | Residue |
| C | PRO78 |
| C | GLY79 |
| C | GLU81 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 352 |
| Chain | Residue |
| C | VAL257 |
| C | MET229 |
| C | GLY234 |
| C | ALA235 |
| C | LYS255 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 353 |
| Chain | Residue |
| C | VAL158 |
| C | ASP159 |
| C | LEU162 |
| C | GLU298 |
| C | THR299 |
| C | THR302 |
| site_id | BC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD D 503 |
| Chain | Residue |
| C | ILE282 |
| D | GLY175 |
| D | GLY177 |
| D | PRO178 |
| D | LEU179 |
| D | GLY180 |
| D | SER198 |
| D | GLU199 |
| D | PRO200 |
| D | ARG204 |
| D | PRO219 |
| D | PHE243 |
| D | SER244 |
| D | ALA246 |
| D | LEU266 |
| D | GLY267 |
| D | LEU268 |
| D | ILE291 |
| D | THR292 |
| D | HOH360 |
| D | HOH361 |
| D | HOH374 |
| D | HOH419 |
| D | HOH443 |
| D | HOH444 |
| D | HOH633 |
| D | HOH634 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 351 |
| Chain | Residue |
| A | ARG271 |
| A | GLU272 |
| D | ARG271 |
| D | HOH610 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 352 |
| Chain | Residue |
| A | PRO270 |
| A | ARG271 |
| D | ARG271 |
| D | GLU272 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEvAGEvvevGpgV |
| Chain | Residue | Details |
| A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00627 |
| Chain | Residue | Details |
| A | THR44 | |
| A | HIS47 | |
| B | THR44 | |
| B | HIS47 | |
| C | THR44 | |
| C | HIS47 | |
| D | THR44 | |
| D | HIS47 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00627 |
| Chain | Residue | Details |
| A | CYS42 | |
| B | GLU68 | |
| B | CYS97 | |
| B | CYS100 | |
| B | CYS103 | |
| B | CYS111 | |
| C | CYS42 | |
| C | HIS67 | |
| C | GLU68 | |
| C | CYS97 | |
| C | CYS100 | |
| A | HIS67 | |
| C | CYS103 | |
| C | CYS111 | |
| D | CYS42 | |
| D | HIS67 | |
| D | GLU68 | |
| D | CYS97 | |
| D | CYS100 | |
| D | CYS103 | |
| D | CYS111 | |
| A | GLU68 | |
| A | CYS97 | |
| A | CYS100 | |
| A | CYS103 | |
| A | CYS111 | |
| B | CYS42 | |
| B | HIS67 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19616102 |
| Chain | Residue | Details |
| A | LEU179 | |
| A | GLU199 | |
| B | LEU179 | |
| B | GLU199 | |
| C | LEU179 | |
| C | GLU199 | |
| D | LEU179 | |
| D | GLU199 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19616102, ECO:0007744|PDB:3GFB |
| Chain | Residue | Details |
| A | ARG204 | |
| D | ARG204 | |
| D | LEU266 | |
| D | ILE291 | |
| A | LEU266 | |
| A | ILE291 | |
| B | ARG204 | |
| B | LEU266 | |
| B | ILE291 | |
| C | ARG204 | |
| C | LEU266 | |
| C | ILE291 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom => ECO:0000255|HAMAP-Rule:MF_00627 |
| Chain | Residue | Details |
| A | GLU152 | |
| B | GLU152 | |
| C | GLU152 | |
| D | GLU152 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | THR44 | |
| A | GLY43 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| B | THR44 | |
| B | GLY43 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| C | THR44 | |
| C | GLY43 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| D | THR44 | |
| D | GLY43 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | THR44 | |
| A | HIS47 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| B | THR44 | |
| B | HIS47 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| C | THR44 | |
| C | HIS47 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| D | THR44 | |
| D | HIS47 |
