Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T44818 Target Info
Target Name Tryptophan 2,3-dioxygenase (TDO)
Synonyms Tryptophanase; Tryptophan pyrrolase; Tryptophan oxygenase; Tryptamin 2,3-dioxygenase; TRPO; TO
Target Type Clinical trial Target
Gene Name TDO2
Biochemical Class Oxygenase
UniProt ID
T23O_HUMAN
Ligand General Information  Top
Ligand Name (S)-3-(5-Fluoro-1H-indol-3-YL)pyrrolidine-2,5-dione Ligand Info
Canonical SMILES C1C(C(=O)NC1=O)C2=CNC3=C2C=C(C=C3)F
InChI 1S/C12H9FN2O2/c13-6-1-2-10-7(3-6)9(5-14-10)8-4-11(16)15-12(8)17/h1-3,5,8,14H,4H2,(H,15,16,17)/t8-/m0/s1
InChIKey MXKLDYKORJEOPR-QMMMGPOBSA-N
PubChem Compound ID 118511968
Drug Binding Sites of Target  Top
PDB ID: 6PYZ      Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PF-06840003 in Active Site
Method X-ray diffraction Resolution 2.02 Å Mutation No [1]
PDB Sequence
GLIYGNYLHL
48
EKVLNAQELQ
58
SETKGNKIHD
68
EHLFIITHQA
78
YELWFKQILW
88

ELDSVREIFQ
98
NGHVRDERNM
108
LKVVSRMHRV
118
SVILKLLVQQ
128
FSILETMTAL
138

DFNDFREYLS
148
PASGFQSLQF
158
RLLENKIGVL
168
QNMRVPYNRR
178
HYRDNFKGEE
188

NELLLKSEQE
198
KTLLELVEAW
208
LERTPGLEPH
218
GFNFWGKLEK
228
NITRGLEEEF
238

IRIQAKEESE
248
EKEEQVAEFQ
258
KQKEVLLSLF
268
DEKRHEHLLS
278
KGERRLSYRA
288

LQGALMIYFY
298
REEPRFQVPF
308
QLLTSLMDID
318
SLMTKWRYNH
328
VCMVHRMLGS
338

KAGTGGSSGY
348
HYLRSTVSDR
358
YKVFVDLFNL
368
STYLIPRHWI
378
PKMNPTIHKF
388

LEH
Residue
Distance (Å)
PHE72
3.417
HIS76
3.017
PHE140
3.658
ARG144
2.564
LEU147
3.931
ALA150
2.934
Residue
Distance (Å)
SER151
2.604
GLY152
3.878
LEU336
3.693
GLY341
3.979
THR342
2.981
GLY343
4.315
PDB ID: 6PYY      Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PF-06840003 in Active Site and Exo site
Method X-ray diffraction Resolution 2.40 Å Mutation No [1]
PDB Sequence
GGLIYGNYLH
47
LEKVLNAQEL
57
QSETKGNKIH
67
DEHLFIITHQ
77
AYELWFKQIL
87

WELDSVREIF
97
QNGHVRDERN
107
MLKVVSRMHR
117
VSVILKLLVQ
127
QFSILETMTA
137

LDFNDFREYL
147
SPASGFQSLQ
157
FRLLENKIGV
167
LQNMRVPYNR
177
RHYRDNFKGE
187

ENELLLKSEQ
197
EKTLLELVEA
207
WLERTPGLEP
217
HGFNFWGKLE
227
KNITRGLEEE
237

FIRIQAKEES
247
EEKEEQVAEF
257
QKQKEVLLSL
267
FDEKRHEHLL
277
SKGERRLSYR
287

ALQGALMIYF
297
YREEPRFQVP
307
FQLLTSLMDI
317
DSLMTKWRYN
327
HVCMVHRMLG
337

SKAGTGGSSG
347
YHYLRSTVSD
357
RYKVFVDLFN
367
LSTYLIPRHW
377
IPKMNPTIHK
387

F
Residue
Distance (Å)
PHE72
3.427
HIS76
3.141
VAL102
4.002
ARG103
2.886
ASP104
4.894
GLU105
2.332
PHE140
3.935
ARG144
2.908
LEU147
3.880
ALA150
3.271
SER151
2.973
GLY152
3.884
TRP208
2.703
Residue
Distance (Å)
LEU209
4.521
ARG211
2.838
THR212
3.668
PRO213
3.357
ILE295
4.040
ARG303
2.878
PHE304
3.512
PRO307
3.858
LEU336
3.414
GLY341
4.103
THR342
2.985
GLY343
4.758
References  Top
REF 1 Structural Basis of Inhibitor Selectivity in Human Indoleamine 2,3-Dioxygenase 1 and Tryptophan Dioxygenase. J Am Chem Soc. 2019 Nov 27;141(47):18771-18779.

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