Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T62390 | Target Info | |||
| Target Name | Tyrosine 3-monooxygenase (TH) | ||||
| Synonyms | Tyrosine 3-hydroxylase; TH | ||||
| Target Type | Successful Target | ||||
| Gene Name | TH | ||||
| Biochemical Class | Paired donor oxygen oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Dopamine | Ligand Info | |||
| Canonical SMILES | C1=CC(=C(C=C1CCN)O)O | ||||
| InChI | 1S/C8H11NO2/c9-4-3-6-1-2-7(10)8(11)5-6/h1-2,5,10-11H,3-4,9H2 | ||||
| InChIKey | VYFYYTLLBUKUHU-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 681 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6ZVP Atomic model of the EM-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms | ||||||
| Method | Electron microscopy | Resolution | 4.00 Å | Mutation | No | [1] |
| PDB Sequence |
SLIEDARKER
49 EAAVAAAAAA59 VPSEPGDPLE69 AVAFEEKEGK79 AMLNLLFSPR89 ATKPSALSRA 99 VKVFETFEAK109 IHHLETRPAQ119 RPRAGGPHLE129 YFVRLEVRRG139 DLAALLSGVR 149 QVSEDVRSPA159 GPKVPWFPRK169 VSELDKCHHL179 VTKFDPDLDL189 DHPGFSDQVY 199 RQRRKLIAEI209 AFQYRHGDPI219 PRVEYTAEEI229 ATWKEVYTTL239 KGLYATHACG 249 EHLEAFALLE259 RFSGYREDNI269 PQLEDVSRFL279 KERTGFQLRP289 VAGLLSARDF 299 LASLAFRVFQ309 CTQYIRHASS319 PMHSPEPDCC329 HELLGHVPML339 ADRTFAQFSQ 349 DIGLASLGAS359 DEEIEKLSTL369 YWFTVEFGLC379 KQNGEVKAYG389 AGLLSSYGEL 399 LHCLSEEPEI409 RAFDPEAAAV419 QPYQDQTYQS429 VYFVSESFSD439 AKDKLRSYAS 449 RIQRPFSVKF459 DPYTLAIDVL469 DSPQAVRRSL479 EGVQDELDTL489 AHALSAIG |
|||||
|
|
||||||
| PDB ID: 6ZN2 Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding. | ||||||
| Method | Electron microscopy | Resolution | 4.30 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
VPWFPRKVSE 172 LDKCHHLVTK182 FDPDLDLDHP192 GFSDQVYRQR202 RKLIAEIAFQ212 YRHGDPIPRV 222 EYTAEEIATW232 KEVYTTLKGL242 YATHACGEHL252 EAFALLERFS262 GYREDNIPQL 272 EDVSRFLKER282 TGFQLRPVAG292 LLSARDFLAS302 LAFRVFQCTQ312 YIRHASSPMH 322 SPEPDCCHEL332 LGHVPMLADR342 TFAQFSQDIG352 LASLGASDEE362 IEKLSTLYWF 372 TVEFGLCKQN382 GEVKAYGAGL392 LSSYGELLHC402 LSEEPEIRAF412 DPEAAAVQPY 422 QDQTYQSVYF432 VSESFSDAKD442 KLRSYASRIQ452 RPFSVKFDPY462 TLAIDVLDSP 472 QAVRRSLEGV482 QDELDTLAHA492 LSAIG> Chain B SLIEDARKER 49 EAAVAAAA
|
|||||
|
|
||||||
| PDB ID: 7PIM Partial structure of tyrosine hydroxylase lacking the first 35 residues in complex with dopamine. | ||||||
| Method | Electron microscopy | Resolution | 4.60 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain B
VPWFPRKVSE 172 LDKCHHLVTK182 FDPDLDLDHP192 GFSDQVYRQR202 RKLIAEIAFQ212 YRHGDPIPRV 222 EYTAEEIATW232 KEVYTTLKGL242 YATHACGEHL252 EAFALLERFS262 GYREDNIPQL 272 EDVSRFLKER282 TGFQLRPVAG292 LLSARDFLAS302 LAFRVFQCTQ312 YIRHASSPMH 322 SPEPDCCHEL332 LGHVPMLADR342 TFAQFSQDIG352 LASLGASDEE362 IEKLSTLYWF 372 TVEFGLCKQN382 GEVKAYGAGL392 LSSYGELLHC402 LSEEPEIRAF412 DPEAAAVQPY 422 QDQTYQSVYF432 VSESFSDAKD442 KLRSYASRIQ452 RPFSVKFDPY462 TLAIDVLDSP 472 QAVRRSLEGV482 QDELDTLAHA492 LSAIG> Chain G SLIEDARKER 49 EAAVAAAA
|
|||||
|
|
||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation. Nat Commun. 2022 Jan 10;13(1):74. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.