6ZVP: Tyrosine 3-monooxygenase

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. Determined by electron microscopy at 4.0 Å resolution. Released 17 Nov 2021.

Method: Electron microscopy
Resolution: 4.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 14,552
Mol. weight: 206.44 kDa
Ligands: LDP, FE
Released: 17 Nov 2021

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

Secondary structure: helices and β-sheets

6ZVP contains 84 α-helices and 56 β-strands across 4 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, B, C and D: 21 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	41-57	17
β-strand	73-76	4	5
β-strand	79-82	4	5
α-helix	96-103	8
α-helix	104-106	3
β-strand	109-115	7	5
β-strand	132-137	6	5
α-helix	138-148	11
β-strand	169	1	6
α-helix	170-179	10
α-helix	197-211	15
α-helix	218-221	4
α-helix	226-243	18
β-strand	247	1	7
α-helix	249-261	13
α-helix	273-282	10
β-strand	286-289	4	8
α-helix	296-304	9
β-strand	307-310	4	8
α-helix	328-330	3
α-helix	331-335	5
α-helix	336-339	4
α-helix	342-355	14
α-helix	360-370	11
α-helix	371-375	5
β-strand	378-381	4	7
β-strand	384-387	4	7
α-helix	396-402	7
β-strand	408-411	4	7
α-helix	414-419	6
β-strand	430-433	4	7
α-helix	437-450	14
β-strand	456-460	5	6
β-strand	465-469	5	6
α-helix	472-495	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine 3-monooxygenase	A, B, C, D	protein	458	Homo sapiens	P07101 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6ZVP_1 Tyrosine 3-monooxygenase (chains A, B, C, D)
SLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAMLNLLFSPRATKPSALSRA
VKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPA
GPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPI
PRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFL
KERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPML
ADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGEL
LHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKF
DPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG

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).
7A2G 4.1 Å, Full-length structure of the substrate-free tyrosine hydroxylase (apo-TH).
6ZN2 4.3 Å, Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic…
7PIM 4.6 Å, Partial structure of tyrosine hydroxylase lacking the first 35 residues in complex with…

Browse structure collections

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