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	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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site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by CaMK2 and PKA","evidences":[{"source":"PubMed","id":"1680128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901013","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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