Structure of PDB 5j6d Chain B

Receptor sequence
>5j6dB (length=248) Species: 9606 (Homo sapiens) [Search protein sequence]
METVPWFPKKISDLDHCANRVLMYGSELDDNVYRKRRKYFADLAMNYKHP
IPKVKTWGTVFQELNKLYPTHACREYLKNLPLLLEDVSNFLKERTGFSIR
PVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPL
LAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCRVFGAGLLS
SISELKHALSKVKPFDPKITCKQECLITTFQDVYFFEDAKEKMREFTK
3D structure
PDB5j6d Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors.
ChainB
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) H142 H147 E187 S200
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 6H5 B M102 T104 M1 T3 MOAD: ic50=6nM
BS02 FE B H272 H277 E317 H142 H147 E187
BS03 6H5 B L129 Y235 L236 R257 Y264 T265 P268 H272 Y312 F313 E317 S336 I366 L28 Y105 L106 R127 Y134 T135 P138 H142 Y182 F183 E187 S200 I227 MOAD: 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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