7A2G

Full-length structure of the substrate-free tyrosine hydroxylase (apo-TH).

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
A	PRO326-PRO337

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04177","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Site: {"description":"Important for substrate specificity","evidences":[{"source":"UniProtKB","id":"P04177","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24529","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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