6ZN2: Partial structure of tyrosine hydroxylase

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. Determined by electron microscopy at 4.3 Å resolution. Released 8 Dec 2021.

Method: Electron microscopy
Resolution: 4.3 Å
Organism: Homo sapiens
Chains: 8
Atoms: 11,320
Mol. weight: 160.68 kDa
Ligands: LDP, FE
Released: 8 Dec 2021

Explore 6ZN2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ZN2 contains 80 α-helices and 40 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, C, E and G: 18 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	169	1	1
α-helix	170-179	10
α-helix	197-211	15
α-helix	218-221	4
α-helix	226-243	18
β-strand	247	1	2
α-helix	249-257	9
α-helix	258-262	5
α-helix	273-282	10
α-helix	285	1
β-strand	286-289	4	3
α-helix	296-304	9
β-strand	307-310	4	3
α-helix	328-334	7
α-helix	342-354	13
α-helix	360-370	11
α-helix	371-375	5
β-strand	378-380	3	2
β-strand	385-387	3	2
α-helix	392-394	3
α-helix	396-402	7
β-strand	408-411	4	2
α-helix	414-417	4
β-strand	430-434	5	2
α-helix	437-450	14
β-strand	456-460	5	1
β-strand	465-469	5	1
α-helix	472-495	24

Chains B, D, F and H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	41-46	6
α-helix	48-56	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine 3-monooxygenase	A, C, E, G	protein	335	Homo sapiens	P07101 (AlphaFold model)
Ser-leu-ile-glu-asp-ala-arg-lys-glu-arg-glu-ala-ala-val-ala-ala-ala-ala	B, D, F, H	protein	18	Homo sapiens	P07101 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>6ZN2_1 Tyrosine 3-monooxygenase (chains A, C, E, G)
VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRV
EYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKER
TGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADR
TFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHC
LSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG

Sequence of entity 2 (B, D, F, H), FASTA

>6ZN2_2 SER-LEU-ILE-GLU-ASP-ALA-ARG-LYS-GLU-ARG-GLU-ALA-ALA-VAL-ALA-ALA-ALA-ALA (chains B, D, F, H)
SLIEDARKEREAAVAAAA

Ligands and cofactors

ID	Name	Formula	Copies
LDP	L-dopamine	C8 H11 N O2	4
FE	FE (III) ion	Fe	4

Primary citation

Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation. Bueno-Carrasco, M.T., Cuellar, J., Flydal, M.I. et al. Nat Commun (2022) 13:74-74. DOI 10.1038/s41467-021-27657-y · PubMed

Other PDB entries of the same protein (UniProt P07101 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2XSN 2.68 Å, Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain
4J6S 3.08 Å, 14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43)
6ZZU 3.5 Å, Partial structure of the substrate-free tyrosine hydroxylase (apo-TH).
6ZVP 4.0 Å, Atomic model of the EM-based structure of the full-length tyrosine hydroxylase in…
7A2G 4.1 Å, Full-length structure of the substrate-free tyrosine hydroxylase (apo-TH).
7PIM 4.6 Å, Partial structure of tyrosine hydroxylase lacking the first 35 residues in complex with…

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