Structure of PDB 6pah Chain A

Receptor sequence
>6pahA (length=308) Species: 9606 (Homo sapiens) [Search protein sequence]
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAY
NYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKY
CGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCT
QYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDE
YIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLP
LELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDP
YTQRIEVL
3D structure
PDB6pah Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
BS02 DAH A H285 H290 Y325 E330 H169 H174 Y209 E214
Gene Ontology
Molecular Function
GO:0004497 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
Biological Process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6pah, PDBe:6pah, PDBj:6pah
PDBsum6pah
PubMed9843368
UniProtP00439|PH4H_HUMAN Phenylalanine-4-hydroxylase (Gene Name=PAH)

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