Structure of PDB 6zn2 Chain E Binding Site BS01
Receptor Information
>6zn2 Chain E (length=335) Species:
9606
(Homo sapiens) [
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VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQ
YRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFS
GYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQ
YIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEE
IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAF
DPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
Ligand information
>6zn2 Chain F (length=18) Species:
9606
(Homo sapiens) [
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SLIEDARKEREAAVAAAA
Receptor-Ligand Complex Structure
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PDB
6zn2
Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Resolution
4.3 Å
Binding residue
(original residue number in PDB)
A296 E364 S367 Y370 W371 Y422
Binding residue
(residue number reindexed from 1)
A134 E202 S205 Y208 W209 Y260
Enzymatic activity
Enzyme Commision number
1.14.16.2
: tyrosine 3-monooxygenase.
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
PDBsum
6zn2
PubMed
35013193
UniProt
P07101
|TY3H_HUMAN Tyrosine 3-monooxygenase (Gene Name=TH)
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