Structure of PDB 4anp Chain A

Receptor sequence
>4anpA (length=309) Species: 9606 (Homo sapiens) [Search protein sequence]
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAY
NYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKY
CGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCT
QYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDE
YIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLP
LELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDP
YTQRIEVLD
3D structure
PDB4anp Structural and Mechanistic Basis of the Interaction between a Pharmacological Chaperone and Human Phenylalanine Hydroxylase.
ChainA
Resolution2.11 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 3QI A F254 P279 P281 H285 W326 E330 F138 P163 P165 H169 W210 E214 MOAD: Ki=200uM
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:4anp, PDBe:4anp, PDBj:4anp
PDBsum4anp
PubMed22549968
UniProtP00439|PH4H_HUMAN Phenylalanine-4-hydroxylase (Gene Name=PAH)

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