Structure of PDB 4q3y Chain A

Receptor sequence

>4q3yA (length=269) Species: 243365 (Chromobacterium violaceum ATCC 12472)

FVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLP
GRACDEFLEGLERLEVDADRVPDFNKLNEKLMAATGWKIVAVPGLIPDDV
FFEHLANRRFPVTWWLREPPDVFHALFGHVPLLINPVFADYLEAYGKGGV
KAKALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDS
ASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFKQLFDATAPDFAPLYLQ
LADAQPWGAGDIAPDDLVL

3D structure

• PDB: 4q3y A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis.
• Chain: A
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H138 H143 E184 S203
• Catalytic site (residue number reindexed from 1): H124 H129 E170 S189
• 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	CO	A	H138 H143 E184	H124 H129 E170

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0004505 phenylalanine 4-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
• GO:0046872 metal ion binding

Biological Process

• GO:0006559 L-phenylalanine catabolic process
• GO:0009072 aromatic amino acid metabolic process
• GO:0019293 tyrosine biosynthetic process, by oxidation of phenylalanine

External links

• PDB: RCSB:4q3y, PDBe:4q3y, PDBj:4q3y
• PDBsum: 4q3y
• PubMed: 25295853
• UniProt: P30967|PH4H_CHRVO Phenylalanine-4-hydroxylase (Gene Name=phhA)