2XSN: Human Tyrosine Hydroxylase Catalytic Domain

Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain. Determined by X-ray diffraction at 2.68 Å resolution. Released 17 Nov 2010.

Method: X-ray diffraction
Resolution: 2.68 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 10,951
Mol. weight: 156.6 kDa
Ligands: ZN
Released: 17 Nov 2010

Explore 2XSN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2XSN contains 87 α-helices and 60 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: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	194	1	1
α-helix	195-196	2
β-strand	200	1	2
α-helix	201-206	6
α-helix	209	1
β-strand	210	1	3
α-helix	211	1
α-helix	228-243	16
α-helix	249-252	4
α-helix	257-277	21
β-strand	278	1	4
α-helix	280-292	13
β-strand	296	1	5
β-strand	299	1	5
α-helix	300-302	3
α-helix	303-314	12
β-strand	317-320	4	6
α-helix	324	1
β-strand	325	1	3
α-helix	326	1
α-helix	327-334	8
β-strand	338-341	4	6
α-helix	359-361	3
α-helix	362-366	5
α-helix	367-370	4
α-helix	373-386	14
α-helix	391-401	11
α-helix	402-406	5
β-strand	409-412	4	4
β-strand	415-418	4	4
α-helix	421-424	4
α-helix	427-433	7
β-strand	439-442	4	4
α-helix	445-449	5
β-strand	461-465	5	4
α-helix	468-480	13
β-strand	487-491	5	2
β-strand	496-500	5	2
α-helix	503-526	24

Chain B: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	194	1	7
α-helix	195-196	2
β-strand	200	1	8
α-helix	201-206	6
α-helix	209	1
β-strand	210	1	9
α-helix	211	1
α-helix	228-243	16
α-helix	249-252	4
α-helix	257-277	21
β-strand	278	1	10
α-helix	280-292	13
β-strand	296	1	11
β-strand	299	1	11
α-helix	300-302	3
α-helix	303-314	12
β-strand	317-320	4	12
α-helix	324	1
β-strand	325	1	9
α-helix	326	1
α-helix	327-334	8
β-strand	338-341	4	12
α-helix	359-361	3
α-helix	362-366	5
α-helix	367-370	4
α-helix	373-386	14
α-helix	391-401	11
α-helix	402-406	5
β-strand	409-412	4	10
β-strand	415-418	4	10
α-helix	421-424	4
α-helix	427-433	7
β-strand	439-442	4	10
α-helix	445-449	5
β-strand	461-465	5	10
α-helix	468-480	13
β-strand	487-491	5	8
β-strand	496-500	5	8
α-helix	503-527	25

Chain C: 19 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	200	1	13
α-helix	201-206	6
β-strand	210	1	14
α-helix	229-243	15
α-helix	249-252	4
α-helix	257-277	21
β-strand	278	1	15
α-helix	280-292	13
β-strand	296	1	16
β-strand	299	1	16
α-helix	300-302	3
α-helix	303-313	11
β-strand	317-320	4	17
β-strand	325	1	14
α-helix	327-334	8
β-strand	338-341	4	17
α-helix	359-361	3
α-helix	362-366	5
α-helix	367-370	4
α-helix	373-386	14
α-helix	391-401	11
α-helix	402-406	5
β-strand	409-412	4	15
β-strand	415-418	4	15
α-helix	421-424	4
α-helix	427-433	7
β-strand	439-442	4	15
α-helix	445-449	5
β-strand	461-465	5	15
α-helix	468-480	13
β-strand	487-491	5	13
β-strand	496-500	5	13
α-helix	503-526	24
β-strand	534	1	7

Chain D: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	200	1	18
α-helix	201-206	6
β-strand	210-211	2	19
α-helix	228-243	16
α-helix	249-252	4
α-helix	257-277	21
β-strand	278	1	20
α-helix	280-292	13
β-strand	296	1	21
β-strand	299	1	21
α-helix	300-302	3
α-helix	303-314	12
β-strand	317-320	4	22
β-strand	324-325	2	19
α-helix	326	1
α-helix	327-334	8
β-strand	338-341	4	22
α-helix	359-360	2
α-helix	361-366	6
α-helix	368-371	4
α-helix	373-386	14
α-helix	391-401	11
α-helix	402-406	5
β-strand	409-412	4	20
β-strand	415-418	4	20
α-helix	421-424	4
α-helix	427-433	7
β-strand	439-442	4	20
α-helix	445-449	5
β-strand	461-465	5	20
α-helix	468-480	13
β-strand	487-491	5	18
β-strand	496-500	5	18
α-helix	503-526	24
β-strand	534	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine 3-monooxygenase	A, B, C, D	protein	343	HOMO SAPIENS	P07101 (AlphaFold model)

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

>2XSN_1 TYROSINE 3-MONOOXYGENASE (chains A, B, C, D)
MVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPR
VEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKE
RTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLAD
RTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLH
CLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDP
YTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIGAENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Primary citation

Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain. Muniz, J.R.C., Cooper, C.D.O., Yue, W.W. et al. To be published.

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

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).
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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