6ZN2

Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0009072	biological_process	aromatic amino acid metabolic process
A	0016714	molecular_function	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
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0009072	biological_process	aromatic amino acid metabolic process
C	0016714	molecular_function	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
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0009072	biological_process	aromatic amino acid metabolic process
E	0016714	molecular_function	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
G	0004497	molecular_function	monooxygenase activity
G	0005506	molecular_function	iron ion binding
G	0009072	biological_process	aromatic amino acid metabolic process
G	0016714	molecular_function	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

Functional Information from PROSITE/UniProt

site_id	PS00367
Number of Residues	12
Details	BH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDccHELLGHVP

Chain	Residue	Details
A	PRO326-PRO337

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: Phosphoserine; by CaMK2 and PKA => ECO:0000269|PubMed:1680128, ECO:0000269|PubMed:7901013

Chain	Residue	Details
B	SER40
G	HIS330
G	HIS335
G	GLU375
D	SER40
F	SER40
H	SER40
C	HIS335
C	GLU375
E	HIS330
E	HIS335
E	GLU375

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site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Important for substrate specificity => ECO:0000250|UniProtKB:P04177

Chain	Residue	Details
A	ASP424
C	ASP424
E	ASP424
G	ASP424

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24529

Chain	Residue	Details
A	SER471
C	SER471
E	SER471
G	SER471

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