Structure of PDB 5fgj Chain A Binding Site BS01

Receptor Information
>5fgj Chain A (length=428) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRP
SRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVP
WFPRTIQELDRFANQILAELDADHPGFKDPVYRARRKQFADIAYNYRHGQ
PIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFRED
NIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHG
SKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLA
TIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKT
ACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVE
VLDNTQQLKILADSINSEVGILCNALQK
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain5fgj Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5fgj Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
Resolution3.6 Å
Binding residue
(original residue number in PDB)		H285 H290 E330
Binding residue
(residue number reindexed from 1)		H263 H268 E308
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H285 H290 E330 S349
Catalytic site (residue number reindexed from 1) H263 H268 E308 S327
Enzyme Commision number 1.14.16.1: phenylalanine 4-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004505 phenylalanine 4-monooxygenase activity
GO:0005506 iron ion binding
GO:0016597 amino acid 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:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006558 L-phenylalanine metabolic process
GO:0006559 L-phenylalanine catabolic process
GO:0006571 tyrosine biosynthetic process
GO:0009072 aromatic amino acid metabolic process
GO:0019293 tyrosine biosynthetic process, by oxidation of phenylalanine

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5fgj, PDBe:5fgj, PDBj:5fgj
PDBsum5fgj
PubMed27145334
UniProtP04176|PH4H_RAT Phenylalanine-4-hydroxylase (Gene Name=Pah)

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