Structure of PDB 6zn2 Chain E

Receptor sequence
>6zn2E (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQ
YRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFS
GYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQ
YIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEE
IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAF
DPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
3D structure
PDB6zn2 Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
ChainE
Resolution4.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.16.2: tyrosine 3-monooxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide E A296 E364 S367 Y370 W371 Y422 A134 E202 S205 Y208 W209 Y260
BS02 LDP E P326 H335 E375 P164 H173 E213
BS03 FE E H330 H335 E375 H168 H173 E213
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6zn2, PDBe:6zn2, PDBj:6zn2
PDBsum6zn2
PubMed35013193
UniProtP07101|TY3H_HUMAN Tyrosine 3-monooxygenase (Gene Name=TH)

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