Structure of PDB 6zn2 Chain G Binding Site BS02
Receptor Information
>6zn2 Chain G (length=335) Species:
9606
(Homo sapiens) [
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VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQ
YRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFS
GYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQ
YIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEE
IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAF
DPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
Ligand information
Ligand ID
LDP
InChI
InChI=1S/C8H11NO2/c9-4-3-6-1-2-7(10)8(11)5-6/h1-2,5,10-11H,3-4,9H2
InChIKey
VYFYYTLLBUKUHU-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
NCCc1ccc(O)c(O)c1
OpenEye OEToolkits 1.5.0
c1cc(c(cc1CCN)O)O
ACDLabs 10.04
Oc1ccc(cc1O)CCN
Formula
C8 H11 N O2
Name
L-DOPAMINE;
DOPAMINE
ChEMBL
CHEMBL59
DrugBank
DB00988
ZINC
ZINC000000033882
PDB chain
6zn2 Chain G Residue 501 [
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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)
P326 H335 E375
Binding residue
(residue number reindexed from 1)
P164 H173 E213
Annotation score
2
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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