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- SASDBZ4: Tyrosine hydroxylase (Isoform 1, Homo sapiens) (Tyrosine hydroxyl... -

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Basic information

Entry
Database: SASBDB / ID: SASDBZ4
SampleTyrosine hydroxylase (Isoform 1, Homo sapiens)
  • Tyrosine hydroxylase, isoform 1 (protein), TYH, Homo sapiens
Function / homology
Function and homology information


tyrosine 3-monooxygenase / tyrosine 3-monooxygenase activity / phytoalexin metabolic process / dopamine biosynthetic process from tyrosine / phthalate metabolic process / glycoside metabolic process / terpene metabolic process / isoquinoline alkaloid metabolic process / norepinephrine biosynthetic process / embryonic camera-type eye morphogenesis ...tyrosine 3-monooxygenase / tyrosine 3-monooxygenase activity / phytoalexin metabolic process / dopamine biosynthetic process from tyrosine / phthalate metabolic process / glycoside metabolic process / terpene metabolic process / isoquinoline alkaloid metabolic process / norepinephrine biosynthetic process / embryonic camera-type eye morphogenesis / hyaloid vascular plexus regression / epinephrine biosynthetic process / circadian sleep/wake cycle / Catecholamine biosynthesis / aminergic neurotransmitter loading into synaptic vesicle / dopamine binding / response to pyrethroid / eye photoreceptor cell development / response to isolation stress / melanosome membrane / sphingolipid metabolic process / response to ether / synaptic transmission, dopaminergic / tetrahydrobiopterin binding / response to herbicide / mating behavior / dopamine biosynthetic process / amino acid binding / regulation of heart contraction / eating behavior / pigmentation / response to corticosterone / response to zinc ion / cellular response to alkaloid / social behavior / response to immobilization stress / smooth endoplasmic reticulum / response to light stimulus / anatomical structure morphogenesis / cellular response to manganese ion / response to electrical stimulus / heart morphogenesis / response to salt stress / response to amphetamine / visual perception / response to nutrient levels / ferric iron binding / fatty acid metabolic process / learning / response to activity / locomotory behavior / cellular response to glucose stimulus / animal organ morphogenesis / ferrous iron binding / terminal bouton / cytoplasmic side of plasma membrane / cerebral cortex development / memory / cellular response to growth factor stimulus / response to peptide hormone / oxygen binding / cellular response to nicotine / cellular response to xenobiotic stimulus / synaptic vesicle / response to estradiol / heart development / cytoplasmic vesicle / perikaryon / response to ethanol / response to lipopolysaccharide / response to hypoxia / neuron projection / protein domain specific binding / axon / dendrite / perinuclear region of cytoplasm / enzyme binding / mitochondrion / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Tyrosine 3-monooxygenase / Tyrosine hydroxylase, conserved site / Tyrosine 3-monooxygenase, catalytic domain / : / Tyrosine hydroxylase N terminal / Tyrosine 3-monooxygenase-like, ACT domain / Tyrosine 3-monooxygenase-like / Aromatic amino acid hydroxylase, iron/copper binding site / Biopterin-dependent aromatic amino acid hydroxylases signature. / Aromatic amino acid hydroxylase ...Tyrosine 3-monooxygenase / Tyrosine hydroxylase, conserved site / Tyrosine 3-monooxygenase, catalytic domain / : / Tyrosine hydroxylase N terminal / Tyrosine 3-monooxygenase-like, ACT domain / Tyrosine 3-monooxygenase-like / Aromatic amino acid hydroxylase, iron/copper binding site / Biopterin-dependent aromatic amino acid hydroxylases signature. / Aromatic amino acid hydroxylase / Aromatic amino acid hydroxylase, C-terminal / Aromatic amino acid monoxygenase, C-terminal domain superfamily / Aromatic amino acid hydroxylase superfamily / Biopterin-dependent aromatic amino acid hydroxylase / Biopterin-dependent aromatic amino acid hydroxylase family profile. / ACT-like domain
Similarity search - Domain/homology
Tyrosine 3-monooxygenase
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationDate: 2016 Sep
Title: Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme
Authors: Bezem M / Baumann A / Skjærven L / Meyer R / Kursula P / Martinez A
Contact author
  • Lars Skjærven (UiB, University of Bergen, Bergen, Norway)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #548
Type: mix / Radius of dummy atoms: 1.90 A / Symmetry: P222 / Chi-square value: 1.548
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Tyrosine hydroxylase (Isoform 1, Homo sapiens) / Specimen concentration: 1.00-3.00
BufferName: 20 mM Na-HEPES 200 mM NaCl / Concentration: 20.00 mM / pH: 7 / Composition: 200 mM NaCl
Entity #351Name: TYH / Type: protein / Description: Tyrosine hydroxylase, isoform 1 / Formula weight: 55.611 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: P07101
Sequence: MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE AAVAAAAAAV PSEPGDPLEA VAFEEKEGKA VLNLLFSPRA TKPSALSRAV KVFETFEAKI HHLETRPAQR PRAGGPHLEY FVRLEVRRGD LAALLSGVRQ VSEDVRSPAG PKVPWFPRKV ...Sequence:
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE AAVAAAAAAV PSEPGDPLEA VAFEEKEGKA VLNLLFSPRA TKPSALSRAV KVFETFEAKI HHLETRPAQR PRAGGPHLEY FVRLEVRRGD LAALLSGVRQ VSEDVRSPAG PKVPWFPRKV SELDKCHHLV TKFDPDLDLD HPGFSDQVYR QRRKLIAEIA FQYRHGDPIP RVEYTAEEIA TWKEVYTTLK GLYATHACGE HLEAFALLER FSGYREDNIP QLEDVSRFLK ERTGFQLRPV AGLLSARDFL ASLAFRVFQC TQYIRHASSP MHSPEPDCCH ELLGHVPMLA DRTFAQFSQD IGLASLGASD EEIEKLSTLY WFTVEFGLCK QNGEVKAYGA GLLSSYGELL HCLSEEPEIR AFDPEAAAVQ PYQDQTYQSV YFVSESFSDA KDKLRSYASR IQRPFSVKFD PYTLAIDVLD SPQAVRRSLE GVQDELDTLA HALSAIG

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Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: Tyrosine hydroxylase (Isoform 1, homo sapiens) / Measurement date: Jun 14, 2015 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.027 4.8012
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1778 /
MinMax
Q0.0586553 4.75365
P(R) point1 1778
R0 20
Result
Type of curve: merged /
ExperimentalPorod
MW283.8 kDa-
Volume-519.8 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I063330 219 62494.4 124.65
Radius of gyration, Rg4.93 nm0.03 4.74 nm0.33

MinMax
D-20
Guinier point40 95

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