Structure of PDB 5j6d Chain A

Receptor sequence
>5j6dA (length=292) Species: 9606 (Homo sapiens) [Search protein sequence]
METVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADL
AMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLS
KYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFH
CTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGAS
EEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKV
KPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTI
3D structure
PDB5j6d Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors.
ChainA
Resolution1.9 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) H171 H176 E216 S235
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 H171 H176 E216
BS02 6H5 A L129 Y235 L236 R257 Y264 T265 P266 P268 H272 A309 Y312 F313 E317 S336 S337 I366 L28 Y134 L135 R156 Y163 T164 P165 P167 H171 A208 Y211 F212 E216 S235 S236 I265 MOAD: ic50=6nM
PDBbind-CN: -logKd/Ki=8.22,IC50=6nM
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:5j6d, PDBe:5j6d, PDBj:5j6d
PDBsum5j6d
PubMed27146606
UniProtP17752|TPH1_HUMAN Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

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