MolNFT v1 · #172224 · protein
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
6ZVP · Tyrosine 3-monooxygenase: “Atomic model of the EM-based structure of the full-length tyrosine hydroxylase in complex with dopamine…”. Electron microscopy, 2 ligands (LDP, FE), 20 pockets (best druggability 0.83). MolNFT v1 #172224…
- PDB
- 6ZVP
- Type
- protein
- Length
- 1,832 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
- LDP, FE
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A, B, C | Tyrosine 3-monooxygenase (EC 1.14.16.2) | protein | 458 | 45% helix, 12% strand | P07101 |
Ligands and binding sites
- LDP · L-dopamine · ligand · 4 copies · chains D, A, B, C
- FE · Fe (III) ion · metal · 4 copies · chains D, A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 752 | 0.83 | 0.86 | 82 | empty |
| 2 | 693 | 0.82 | 0.86 | 56 | LDP |
| 3 | 679 | 0.82 | 0.86 | 55 | LDP |
| 4 | 663 | 0.82 | 0.86 | 55 | LDP |
| 5 | 674 | 0.81 | 0.85 | 58 | LDP |
Interfaces
6 interfaces between chains.
- D–A · 1955 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1955 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 933 Ų buried · 12 hydrogen bonds · protein-protein
- D–C · 926 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 622 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 6ZVP · Atomic model of the EM-based structure of the full-length tyrosine hydroxylase in complex… · the same entry in another collection · chain D against D, TM-score 1.00
- P07101 · AlphaFold monomer V2.0 prediction for tyrosine 3-monooxygenase (P07101) · a predicted model of the same protein · chain D against A, TM-score 0.82
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 6ZVP · PDBe 6ZVP · UniProt P07101
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