EMD-16223

Single-particle
3.9 Å
EMD-16223 Deposition: 23/11/2022
Map released: 10/05/2023
Last modified: 14/06/2023
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-16223

Cryo-EM structure of the catalytic domain tetramer of N-terminally truncated human tryptophan hydroxylase 2

EMD-16223

Single-particle
3.9 Å
EMD-16223 Deposition: 23/11/2022
Map released: 10/05/2023
Last modified: 14/06/2023
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Homo sapiens
Sample: 47 N-terminally truncated human tryptophan hydroxylase 2

Deposition Authors: Zhang Z , Vedel IM , Skawinska NT, Harris P , Stark H, Peters GHJ
Structural characterization of human tryptophan hydroxylase 2 reveals that L-Phe is superior to L-Trp as the regulatory domain ligand.
Vedel IM , Prestel A, Zhang Z , Skawinska NT, Stark H, Harris P , Kragelund BB, Peters GHJ
(2023) Structure , 31 , 689 - 699.e6
PUBMED: 37119821
DOI: doi:10.1016/j.str.2023.04.004
ISSN: 0969-2126
ASTM: STRUE6