7A2G: Tyrosine 3-monooxygenase

Full-length structure of the substrate-free tyrosine hydroxylase (apo-TH). Determined by electron microscopy at 4.1 Å resolution. Released 1 Dec 2021.

Method: Electron microscopy
Resolution: 4.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,408
Mol. weight: 190.13 kDa
Ligands: FE
Released: 1 Dec 2021

Explore 7A2G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7A2G contains 79 α-helices and 46 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: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	80	1	1
α-helix	99-104	6
β-strand	136	1	1
α-helix	138-151	14
α-helix	175-181	7
α-helix	197-210	14
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
β-strand	286-289	4	3
α-helix	296-304	9
β-strand	307-310	4	3
α-helix	328-331	4
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	2
β-strand	384-387	4	2
α-helix	397-403	7
β-strand	410-411	2	4
α-helix	414-418	5
β-strand	432-433	2	4
α-helix	437-450	14
β-strand	456-459	4	5
β-strand	466-469	4	5
α-helix	472-495	24

Chain B: 20 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	80	1	6
α-helix	99-105	7
β-strand	136	1	6
α-helix	138-151	14
α-helix	175-181	7
α-helix	197-210	14
α-helix	213-214	2
α-helix	219-221	3
α-helix	226-243	18
β-strand	247	1	7
α-helix	249-261	13
α-helix	269-270	2
α-helix	272-282	11
β-strand	286-289	4	8
α-helix	296-304	9
β-strand	307-310	4	8
α-helix	328-334	7
α-helix	336-339	4
α-helix	342-354	13
α-helix	360-370	11
α-helix	371-375	5
β-strand	378	1	9
β-strand	380-381	2	10
β-strand	384-385	2	10
β-strand	387	1	7
α-helix	392-394	3
α-helix	397-403	7
β-strand	409-411	3	9
β-strand	431-433	3	9
α-helix	437-450	14
β-strand	456-459	4	11
β-strand	466-469	4	11
α-helix	472-495	24

Chain C: 20 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	80	1	12
α-helix	99-105	7
β-strand	136	1	12
α-helix	138-151	14
α-helix	171-173	3
α-helix	175-181	7
α-helix	197-210	14
α-helix	219-221	3
α-helix	226-243	18
β-strand	247	1	13
α-helix	249-261	13
α-helix	272-283	12
β-strand	286-289	4	14
α-helix	296-304	9
β-strand	307-310	4	14
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	1	15
β-strand	387	1	13
α-helix	397-403	7
β-strand	409-411	3	15
α-helix	414-418	5
β-strand	431-433	3	15
α-helix	437-450	14
β-strand	456-459	4	16
β-strand	466-469	4	16
α-helix	472-495	24

Chain D: 21 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	80-81	2	17
α-helix	99-105	7
β-strand	135-136	2	17
α-helix	138-151	14
α-helix	171-173	3
α-helix	175-181	7
α-helix	197-210	14
α-helix	213-214	2
α-helix	218-221	4
α-helix	226-243	18
β-strand	247	1	18
α-helix	249-261	13
α-helix	269-270	2
α-helix	273-282	10
β-strand	286-289	4	19
α-helix	296-304	9
β-strand	307-310	4	19
α-helix	328-334	7
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	18
β-strand	384-387	4	18
α-helix	397-403	7
β-strand	409-411	3	20
α-helix	414-418	5
β-strand	431-433	3	20
α-helix	437-450	14
β-strand	456-459	4	21
β-strand	466-469	4	21
α-helix	472-495	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine 3-monooxygenase	A, B, C, D	protein	420	Homo sapiens	P07101 (AlphaFold model)

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

>7A2G_1 Tyrosine 3-monooxygenase (chains A, B, C, D)
GKAMLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVR
RGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQ
VYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFAL
LERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHA
SSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFG
LCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESF
SDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG

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)
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…
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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