Structure of PDB 1pah Chain A

Receptor sequence
>1pahA (length=308) Species: 9606 (Homo sapiens) [Search protein sequence]
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAY
NYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKY
CGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCT
QYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDE
YIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLP
LELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDP
YTQRIEVL
3D structure
PDB1pah Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.
ChainA
Resolution2.0 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) 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: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:1pah, PDBe:1pah, PDBj:1pah
PDBsum1pah
PubMed9406548
UniProtP00439|PH4H_HUMAN Phenylalanine-4-hydroxylase (Gene Name=PAH)

[Back to BioLiP]