6ZZU: Tyrosine 3-monooxygenase

Partial structure of the substrate-free tyrosine hydroxylase (apo-TH). Determined by electron microscopy at 3.5 Å resolution. Released 17 Nov 2021.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,760
Mol. weight: 152.57 kDa
Ligands: FE
Released: 17 Nov 2021

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

Secondary structure: helices and β-sheets

6ZZU contains 78 α-helices and 36 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.

Chain A: 21 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	172-175	4
α-helix	197-208	12
α-helix	218-221	4
α-helix	226-239	14
α-helix	241-243	3
β-strand	247	1	4
α-helix	249-257	9
α-helix	258-262	5
α-helix	269-271	3
α-helix	272-282	11
β-strand	286-289	4	5
α-helix	296-303	8
β-strand	307-310	4	5
α-helix	328-334	7
α-helix	336-339	4
α-helix	342-353	12
α-helix	360-370	11
α-helix	371-375	5
β-strand	378-380	3	4
β-strand	385-387	3	4
α-helix	392-394	3
α-helix	398-402	5
β-strand	408-411	4	4
α-helix	412	1
α-helix	427-428	2
β-strand	430-433	4	4
α-helix	437-449	13
β-strand	456-460	5	6
β-strand	465-469	5	6
α-helix	472-495	24

Chain B: 20 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	171-173	3
α-helix	175-181	7
α-helix	197-207	11
α-helix	218-221	4
α-helix	226-241	16
β-strand	247	1	1
α-helix	249-261	13
α-helix	269-271	3
α-helix	272-282	11
β-strand	286-289	4	2
α-helix	296-304	9
β-strand	307-310	4	2
α-helix	328-330	3
α-helix	331-335	5
α-helix	336-339	4
α-helix	342-354	13
α-helix	360-370	11
α-helix	371-375	5
β-strand	378-381	4	1
β-strand	384-387	4	1
α-helix	396-401	6
β-strand	408-411	4	1
α-helix	412	1
α-helix	427-428	2
β-strand	430-434	5	1
α-helix	437-450	14
β-strand	456-460	5	3
β-strand	465-469	5	3
α-helix	472-495	24

Chain C: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	172-175	4
α-helix	197-207	11
α-helix	218-221	4
α-helix	226-241	16
β-strand	247	1	7
α-helix	249-257	9
α-helix	258-262	5
α-helix	269-271	3
α-helix	272-282	11
β-strand	286-289	4	8
α-helix	296-303	8
β-strand	307-310	4	8
α-helix	328-331	4
α-helix	336-339	4
α-helix	342-353	12
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	412	1
α-helix	427-428	2
β-strand	430-434	5	7
α-helix	437-447	11
β-strand	456-460	5	9
β-strand	465-469	5	9
α-helix	472-495	24

Chain D: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	172-175	4
α-helix	197-208	12
α-helix	218-221	4
α-helix	226-241	16
β-strand	247	1	10
α-helix	249-260	12
α-helix	268-271	4
α-helix	272-282	11
β-strand	286-289	4	11
α-helix	296-303	8
β-strand	307-310	4	11
α-helix	328-331	4
α-helix	336-339	4
α-helix	342-353	12
α-helix	360-370	11
α-helix	371-375	5
β-strand	378-381	4	10
β-strand	384-387	4	10
α-helix	392-394	3
α-helix	398-402	5
β-strand	408-411	4	10
α-helix	412	1
β-strand	430-433	4	10
α-helix	437-450	14
β-strand	456-460	5	12
β-strand	465-469	5	12
α-helix	472-495	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine 3-monooxygenase	A, B, C, D	protein	335	Homo sapiens	P07101 (AlphaFold model)

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

>6ZZU_1 Tyrosine 3-monooxygenase (chains A, B, C, D)
VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRV
EYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKER
TGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADR
TFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHC
LSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG

Ligands and cofactors

ID	Name	Formula	Copies
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)
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).
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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