Structure of PDB 6hpo Chain A

Receptor sequence

>6hpoA (length=310) Species: 9606 (Homo sapiens)

TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAY
NYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKY
CGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCT
QYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDE
YIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLP
LELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDP
YTQRIEVLDN

3D structure

• PDB: 6hpo Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin.
• Chain: A
• Resolution: 1.67 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H285 H290 E330 S349
• Catalytic site (residue number reindexed from 1): H169 H174 E214 S233
• Enzyme Commision number: 1.14.16.1: phenylalanine 4-monooxygenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FE	A	H285 H290 E330	H169 H174 E214

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0004505 phenylalanine 4-monooxygenase activity
• GO:0005506 iron ion binding
• GO:0016714 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
• GO:0046872 metal ion binding

Biological Process

• GO:0006559 L-phenylalanine catabolic process
• GO:0006571 tyrosine biosynthetic process
• GO:0008652 amino acid biosynthetic process
• GO:0009072 aromatic amino acid metabolic process
• GO:0019293 tyrosine biosynthetic process, by oxidation of phenylalanine
• GO:0042423 catecholamine biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:6hpo, PDBe:6hpo, PDBj:6hpo
• PDBsum: 6hpo
• PubMed: 31118288
• UniProt: P00439|PH4H_HUMAN Phenylalanine-4-hydroxylase (Gene Name=PAH)