Structure of PDB 3hf8 Chain A

Receptor sequence
>3hf8A (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
SVPWFPKKISDLDHCANRDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEE
EIKTWGTVFRELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSN
FLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPD
TCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFG
LCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTF
QDVYFVSESFEDAKEKMREFTKTI
3D structure
PDB3hf8 Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H272 H277 E317 S336
Catalytic site (residue number reindexed from 1) H153 H158 E198 S217
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 H153 H158 E198
BS02 ML0 A Y235 L236 S237 P238 R257 Y264 T265 P266 E267 P268 H272 F313 E317 S336 S337 C364 I366 Y116 L117 S118 P119 R138 Y145 T146 P147 E148 P149 H153 F194 E198 S217 S218 C245 I247 MOAD: Ki=0.31uM
PDBbind-CN: -logKd/Ki=6.51,Ki=0.31uM
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:3hf8, PDBe:3hf8, PDBj:3hf8
PDBsum3hf8
PubMed20556201
UniProtP17752|TPH1_HUMAN Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

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