6HPO

Crystallographic structure of the catalytic domain of Human Phenylalanine Hydroxylase (hPAH CD) in complex with iron at 1.6 Angstrom

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0004505	molecular_function	phenylalanine 4-monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005829	cellular_component	cytosol
A	0006559	biological_process	L-phenylalanine catabolic process
A	0006571	biological_process	tyrosine biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
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	0019293	biological_process	tyrosine biosynthetic process, by oxidation of phenylalanine
A	0042423	biological_process	catecholamine biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue FE A 501

Chain	Residue
A	HIS285
A	HIS290
A	GLU330
A	HOH608
A	HOH618
A	HOH809

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO281-PRO292

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P04176

Chain	Residue	Details
A	HIS285
A	HIS290
A	GLU330

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:12185072, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER16

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