› 5j6d

X-ray diffraction
1.9Å resolution

Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors

Released:
DOI: 10.2210/pdb5j6d/pdb
PDB entry 5j6d coloured by chain, front view.
PDB entry 5j6d coloured by chain, side view.
PDB entry 5j6d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors.
Goldberg DR, De Lombaert S, Aiello R, Bourassa P, Barucci N, Zhang Q, Paralkar V, Stein AJ, Valentine J, Zavadoski W
Bioorg Med Chem Lett 26 2855-2860 (2016)
PMID: 27146606

Function and Biology Details

Reaction catalysed: 
L-tryptophan + tetrahydrobiopterin + O(2) = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-148158 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan 5-hydroxylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 307 amino acids
Theoretical weight: 35.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17752 (Residues: 102-402; Coverage: 68%)
Gene names: TPH, TPH1, TPRH, TRPH
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments

4 bound ligands:
Ligand FE 2 x FE
Ligand TRS 2 x TRS
Ligand GOL 2 x GOL
Ligand 6H5 2 x 6H5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 58.726Å b: 63.561Å c: 156.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.248
Expression system: Escherichia coli

Quick links

Citations

3 review citations

5-Hydroxytryptophan (5-HTP): Natural Occurrence, Analysis, Biosynthesis, Biotechnology, Physiology and Toxicology.
Maffei ME. (2020)
2 more