› 8cji

X-ray diffraction
1.65Å resolution

Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-07-052

Released:
DOI: 10.2210/pdb8cji/pdb
PDB entry 8cji coloured by chain, front view.
PDB entry 8cji coloured by chain, side view.
PDB entry 8cji coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Based Design of Xanthine-Imidazopyridines and -Imidazothiazoles as Highly Potent and In Vivo Efficacious Tryptophan Hydroxylase Inhibitors.
Specker E, Wesolowski R, Schütz A, Matthes S, Mallow K, Wasinska-Kalwa M, Winkler L, Oder A, Alenina N, Pleimes D, von Kries JP, Heinemann U, Bader M, Nazaré M
J Med Chem 66 14866-14896 (2023)
PMID: 37905925

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

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: 326 amino acids
Theoretical weight: 37.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17752 (Residues: 105-401; Coverage: 67%)
Gene names: TPH, TPH1, TPRH, TRPH
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand UWC 1 x UWC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 46.84Å b: 57.7Å c: 58.8Å
α: 90° β: 97.66° γ: 90°
R-values:
R R work R free
0.238 0.236 0.265
Expression system: Escherichia coli

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