Crystal structure of human tryptophan hydroxylase type 1 with bound LP-521834 and FE

Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis

SVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFRELNK
LYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPF
YTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKH
ALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTI

1:1 ratio of the concentrated protein solution and a reservoir comprising 24-28% (w/v) PEG 6000, and 100 mM, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 20 CK, temperature 293K

TRYPTOPHAN 5-HYDROXYLASE 1, Alternative splicing, Iron, Metal-binding, Monooxygenase, Oxidoreductase, Phosphoprotein, Serotonin biosynthesis

TVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNK
LYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPF
YTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKH
ALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTI