4PW8: Human Tryptophan 2,3-dioxygenase

Tryptophan 2,3-dioxygenase (TDO), one of the two key enzymes in the kynurenine pathway, catalyzes the indole ring cleavage at the C2-C3 bond of L-tryptophan. This is a rate-limiting step in the regulation of tryptophan concentration in vivo, and is thus important in drug discovery for cancer and immune diseases. Here, we report the crystal structure of human TDO (hTDO) without the heme cofactor to 2.90 A resolution. The overall fold and the tertiary assembly of hTDO into a tetramer, as well as the active site architecture, are well conserved and similar to the structures of known orthologues. Kinetic and mutational studies confirmed that eight residues play critical roles in L-tryptophan oxidation.
PDB ID: 4PW8Download
MMDB ID: 122193
PDB Deposition Date: 2014/3/19
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 4PW8: tetrameric; determined by author and by software (PISA)
Molecular Components in 4PW8
Label Count Molecule
Proteins (4 molecules)
Tryptophan 2,3-dioxygenase(Gene symbol: TDO2)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB