Research workbench
Full-length structure of the substrate-free tyrosine hydroxylase (apo- th).
Analyse Full-length structure of the substrate-free tyrosine hydroxylase (apo- th). in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A2G
- Type
- protein
- Length
- 1,680 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine 3-monooxygenase
- EC
- 1.14.16.2
- UniProt
- P07101
- Ligands
- FE
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 43% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Tyrosine 3-monooxygenase (EC 1.14.16.2) | protein | 420 | 43% helix, 7% strand | P07101 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 736 | 0.82 | 0.85 | 57 | empty |
| 2 | 788 | 0.81 | 0.84 | 73 | empty |
| 3 | 693 | 0.79 | 0.83 | 74 | empty |
| 4 | 129 | 0.79 | 0.96 | 30 | empty |
| 5 | 660 | 0.78 | 0.83 | 73 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1790 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1783 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1159 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1146 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 590 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7A2G · Full-length structure of the substrate-free tyrosine hydroxylase (apo-TH). · the same entry in another collection · chain A against A, TM-score 1.00
- P07101 · AlphaFold monomer V2.0 prediction for tyrosine 3-monooxygenase (P07101) · a predicted model of the same protein · chain A against A, TM-score 0.81
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P07101
- Elsewhere: RCSB PDB 7A2G · PDBe 7A2G · UniProt P07101
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