Structure of PDB 5tpg Chain A

Receptor sequence
>5tpgA (length=271) Species: 9606 (Homo sapiens) [Search protein sequence]
TVPWFPKKISDLDHCNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKT
WGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKE
RTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHE
LLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQ
DGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVY
FVSESFEDAKEKMREFTKTIK
3D structure
PDB5tpg Optimization of spirocyclic proline tryptophan hydroxylase-1 inhibitors.
ChainA
Resolution1.5 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) H149 H154 E194 S213
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 H149 H154 E194
BS02 7H5 A Y235 P238 F241 R257 Y264 T265 P266 E267 A309 Y312 E317 S336 S337 Y112 P115 F118 R134 Y141 T142 P143 E144 A186 Y189 E194 S213 S214 MOAD: ic50=14nM
PDBbind-CN: -logKd/Ki=7.85,IC50=14nM
BindingDB: IC50=14nM
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:5tpg, PDBe:5tpg, PDBj:5tpg
PDBsum5tpg
PubMed28041831
UniProtP17752|TPH1_HUMAN Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

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