› 5tpg

X-ray diffraction
1.5Å resolution

Optimization of spirocyclic proline tryptophanhydroxylase-1 inhibitors

Released:
DOI: 10.2210/pdb5tpg/pdb
PDB entry 5tpg coloured by chain, front view.
PDB entry 5tpg coloured by chain, side view.
PDB entry 5tpg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Optimization of spirocyclic proline tryptophan hydroxylase-1 inhibitors.
Goldberg DR, De Lombaert S, Aiello R, Bourassa P, Barucci N, Zhang Q, Paralkar V, Stein AJ, Holt M, Valentine J, Zavadoski W
Bioorg Med Chem Lett 27 413-419 (2017)
PMID: 28041831

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148158 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan 5-hydroxylase 1 Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 35.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17752 (Residues: 104-402; Coverage: 67%)
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 1 x FE
Ligand TRS 1 x TRS
Ligand CCN 2 x CCN
Ligand 7H5 1 x 7H5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 47.198Å b: 58.161Å c: 51.567Å
α: 90° β: 93.72° γ: 90°
R-values:
R R work R free
0.188 0.187 0.215
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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