Structure of PDB 3hf6 Chain A

Receptor sequence

>3hf6A (length=280) Species: 9606 (Homo sapiens)

SVPWFPKKISDLDHCLDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPK
VEFTEEEIKTWGTVFRELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQ
LEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPF
YTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYF
FTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQE
CLITTFQDVYFVSESFEDAKEKMREFTKTI

3D structure

• PDB: 3hf6 Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H272 H277 E317 S336
• Catalytic site (residue number reindexed from 1): H159 H164 E204 S223
• Enzyme Commision number: 1.14.16.4: tryptophan 5-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	H272 H277 E317	H159 H164 E204
BS02	LX0	A	G234 Y235 R257 Y264 T265 P266 E267 P268 H272 F313 E317 S336 S337	G121 Y122 R144 Y151 T152 P153 E154 P155 H159 F200 E204 S223 S224	MOAD: ic50=0.026uM PDBbind-CN: -logKd/Ki=7.59,IC50=0.026uM BindingDB: IC50=26nM

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

External links

• PDB: RCSB:3hf6, PDBe:3hf6, PDBj:3hf6
• PDBsum: 3hf6
• PubMed: 19631532
• UniProt: P17752|TPH1_HUMAN Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)