Structure of PDB 1j8u Chain A

Receptor sequence
>1j8uA (length=307) Species: 9606 (Homo sapiens) [Search protein sequence]
VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYN
YRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYC
GFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQ
YIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEY
IEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPL
ELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPY
TQRIEVL
3D structure
PDB1j8u High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H285 H290 E330 S349
Catalytic site (residue number reindexed from 1) H168 H173 E213 S232
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 FE2 A H285 H290 E330 H168 H173 E213
BS02 H4B A L249 S251 F254 L255 A322 L132 S134 F137 L138 A205
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1j8u, PDBe:1j8u, PDBj:1j8u
PDBsum1j8u
PubMed11718561
UniProtP00439|PH4H_HUMAN Phenylalanine-4-hydroxylase (Gene Name=PAH)

[Back to BioLiP]