6ZVP

Atomic model of the EM-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0004511	molecular_function	tyrosine 3-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
A	0042423	biological_process	catecholamine biosynthetic process
B	0004497	molecular_function	monooxygenase activity
B	0004511	molecular_function	tyrosine 3-monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0009072	biological_process	aromatic amino acid metabolic process
B	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
B	0042423	biological_process	catecholamine biosynthetic process
C	0004497	molecular_function	monooxygenase activity
C	0004511	molecular_function	tyrosine 3-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
C	0042423	biological_process	catecholamine biosynthetic process
D	0004497	molecular_function	monooxygenase activity
D	0004511	molecular_function	tyrosine 3-monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0009072	biological_process	aromatic amino acid metabolic process
D	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
D	0042423	biological_process	catecholamine biosynthetic process

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
D	PRO326-PRO337

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P04177

Chain	Residue	Details
D	HIS330
C	HIS330
C	HIS335
C	GLU375
D	HIS335
D	GLU375
A	HIS330
A	HIS335
A	GLU375
B	HIS330
B	HIS335
B	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
D	ASP424
A	ASP424
B	ASP424
C	ASP424

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine; by CaMK2 and PKA => ECO:0000269|PubMed:1680128, ECO:0000269|PubMed:7901013

Chain	Residue	Details
D	SER40
A	SER40
B	SER40
C	SER40

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24529

Chain	Residue	Details
D	SER471
A	SER471
B	SER471
C	SER471

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