Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T78915 | Target Info | |||
| Target Name | Tryptophan 5-hydroxylase 1 (TPH1) | ||||
| Synonyms | Tryptophan 5-monooxygenase 1; TRPH; TPRH | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | TPH1 | ||||
| Biochemical Class | Paired donor oxygen oxidoreductase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: KAR5585 | Ligand Info | |||||
| Structure Description | Tryptophan 5-hydroxylase in complex with inhibitor (3~{S})-8-[2-azanyl-6-[(1~{R})-1-(4-chloranyl-2-phenyl-phenyl)-2,2,2-tris(fluoranyl)ethoxy]pyrimidin-4-yl]-2,8-diazaspiro[4.5]decane-3-carboxylic acid | PDB:5L01 | ||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [1] |
| PDB Sequence |
TVPWFPKKIS
113 DLDHCANRVL123 MYGGFKDNVY141 RKRRKYFADL151 AMNYKHGDPI161 PKVEFTEEEI 171 KTWGTVFQEL181 NKLYPTHACR191 EYLKNLPLLS201 KYCGYREDNI211 PQLEDVSNFL 221 KERTGFSIRP231 VAGYLSPRDF241 LSGLAFRVFH251 CTQYVRHSSD261 PFYTPEPDTC 271 HELLGHVPLL281 AEPSFAQFSQ291 EIGLASLGAS301 EEAVQKLATC311 YFFTVEFGLC 321 KQDGQLRVFG331 AGLLSSISEL341 KHALSGHAKV351 KPFDPKITCK361 QECLITTFQD 371 VYFVSESFED381 AKEKMREFTK391 TIK
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LEU123
4.239
TYR235
3.777
LEU236
3.295
SER237
4.242
PRO238
3.818
PHE241
4.213
LEU242
4.922
ARG257
2.635
PHE263
4.586
TYR264
3.395
THR265
2.859
PRO266
3.126
GLU267
3.532
PRO268
3.615
|
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| Ligand Name: 7,8-dihydrobiopterin | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III) | PDB:1MLW | ||||
| Method | X-ray diffraction | Resolution | 1.71 Å | Mutation | No | [2] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVL123 MYGSELDADH133 PGFKDNVYRK143 RRKYFADLAM153 NYKHGDPIPK 163 VEFTEEEIKT173 WGTVFRELNK183 LYPTHACREY193 LKNLPLLSKY203 CGYREDNIPQ 213 LEDVSNFLKE223 RTGFSIRPVA233 GYLSPRDFLS243 GLAFRVFHCT253 QYVRHSSDPF 263 YTPEPDTCHE273 LLGHVPLLAE283 PSFAQFSQEI293 GLASLGASEE303 AVQKLATCYF 313 FTVEFGLCKQ323 DGQLRVFGAG333 LLSSISELKH343 ALSGHAKVKP353 FDPKITCKQE 363 CLITTFQDVY373 FVSESFEDAK383 EKMREFTKTI393
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| Ligand Name: 8-(1~{H}-benzimidazol-2-ylmethyl)-3-ethyl-7-(phenylmethyl)purine-2,6-dione | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor AG-01-128 | PDB:7ZIH | ||||
| Method | X-ray diffraction | Resolution | 1.47 Å | Mutation | No | [3] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVL123 SELDADHPGF136 KDNVYRKRRK146 YFADLAMNYK156 HGDPIPKVEF 166 TEEEIKTWGT176 VFQELNKLYP186 THACREYLKN196 LPLLSKYCGY206 REDNIPQLED 216 VSNFLKERTG226 FSIRPVAGYL236 SPRDFLSGLA246 FRVFHCTQYV256 RHSSDPFYTP 266 EPDTCHELLG276 HVPLLAEPSF286 AQFSQEIGLA296 SLGASEEAVQ306 KLATCYFFTV 316 EFGLCKQDGQ326 LRVFGAGLLS336 SISELKHALS346 GHAKVKPFDP356 KITCKQECLI 366 TTFQDVYFVS376 ESFEDAKEKM386 REFTKTIK
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .JCR or .JCR2 or .JCR3 or :3JCR;style chemicals stick;color identity;select .A:232 or .A:234 or .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:242 or .A:251 or .A:253 or .A:255 or .A:268 or .A:272 or .A:277 or .A:309 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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VAL232
4.282
GLY234
3.633
TYR235
3.246
LEU236
2.760
SER237
3.938
PRO238
3.078
PHE241
3.446
LEU242
4.345
HIS251
4.853
THR253
3.735
|
|||||
| Ligand Name: 8-(5~{H}-[1,3]dioxolo[4,5-f]benzimidazol-6-ylmethyl)-7-(phenylmethyl)-3-propyl-purine-2,6-dione | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-05-193 | PDB:7ZII | ||||
| Method | X-ray diffraction | Resolution | 1.63 Å | Mutation | No | [3] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVL123 ELDADHPGFK137 DNVYRKRRKY147 FADLAMNYKH157 GDPIPKVEFT 167 EEEIKTWGTV177 FQELNKLYPT187 HACREYLKNL197 PLLSKYCGYR207 EDNIPQLEDV 217 SNFLKERTGF227 SIRPVAGYLS237 PRDFLSGLAF247 RVFHCTQYVR257 HSSDPFYTPE 267 PDTCHELLGH277 VPLLAEPSFA287 QFSQEIGLAS297 LGASEEAVQK307 LATCYFFTVE 317 FGLCKQDGQL327 RVFGAGLLSS337 ISELKHALSG347 HAKVKPFDPK357 ITCKQECLIT 367 TFQDVYFVSE377 SFEDAKEKMR387 EFTKTIK
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IVQ or .IVQ2 or .IVQ3 or :3IVQ;style chemicals stick;color identity;select .A:232 or .A:234 or .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:242 or .A:251 or .A:253 or .A:255 or .A:266 or .A:268 or .A:272 or .A:277 or .A:309 or .A:312 or .A:317 or .A:318 or .A:333 or .A:366; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
VAL232
4.125
GLY234
3.587
TYR235
3.243
LEU236
2.678
SER237
3.980
PRO238
3.223
PHE241
3.384
LEU242
4.055
HIS251
4.842
THR253
3.731
TYR255
4.539
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| Ligand Name: (2~{R})-2-azanyl-5-[[2-[[3-methyl-2,6-bis(oxidanylidene)-7-(phenylmethyl)purin-8-yl]methyl]-1~{H}-benzimidazol-5-yl]amino]-5-oxidanylidene-pentanoic acid | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-05-060 | PDB:7ZIG | ||||
| Method | X-ray diffraction | Resolution | 1.81 Å | Mutation | No | [3] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVE128 LDADHPGFKD138 NVYRKRRKYF148 ADLAMNYKHG158 DPIPKVEFTE 168 EEIKTWGTVF178 QELNKLYPTH188 ACREYLKNLP198 LLSKYCGYRE208 DNIPQLEDVS 218 NFLKERTGFS228 IRPVAGYLSP238 RDFLSGLAFR248 VFHCTQYVRH258 SSDPFYTPEP 268 DTCHELLGHV278 PLLAEPSFAQ288 FSQEIGLASL298 GASEEAVQKL308 ATCYFFTVEF 318 GLCKQDGQLR328 VFGAGLLSSI338 SELKHALSGH348 AKVKPFDPKI358 TCKQECLITT 368 FQDVYFVSES378 FEDAKEKMRE388 FTKTI
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IVZ or .IVZ2 or .IVZ3 or :3IVZ;style chemicals stick;color identity;select .A:232 or .A:234 or .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:251 or .A:253 or .A:255 or .A:257 or .A:263 or .A:264 or .A:265 or .A:267 or .A:268 or .A:272 or .A:277 or .A:309 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:366; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
VAL232
4.194
GLY234
3.622
TYR235
3.449
LEU236
2.767
SER237
3.878
PRO238
2.988
PHE241
3.380
HIS251
4.771
THR253
3.682
TYR255
4.316
ARG257
4.401
PHE263
3.573
TYR264
3.291
THR265
3.092
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| Ligand Name: (2R)-2-azanyl-5-[[2-[3-methyl-2,6-bis(oxidanylidene)-7-(phenylmethyl)purin-8-yl]sulfanyl-3H-benzimidazol-5-yl]amino]-5-oxidanylidene-pentanoic acid | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-480 | PDB:7ZIF | ||||
| Method | X-ray diffraction | Resolution | 1.87 Å | Mutation | No | [3] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVL123 MYGSELDADH133 PGFKDNVYRK143 RRKYFADLAM153 NYKHGDPIPK 163 VEFTEEEIKT173 WGTVFQELNK183 LYPTHACREY193 LKNLPLLSKY203 CGYREDNIPQ 213 LEDVSNFLKE223 RTGFSIRPVA233 GYLSPRDFLS243 GLAFRVFHCT253 QYVRHSSDPF 263 YTPEPDTCHE273 LLGHVPLLAE283 PSFAQFSQEI293 GLASLGASEE303 AVQKLATCYF 313 FTVEFGLCKQ323 DGQLRVFGAG333 LLSSISELKH343 ALSGHAKVKP353 FDPKITCKQE 363 CLITTFQDVY373 FVSESFEDAK383 EKMREFTKTI393 K
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IWA or .IWA2 or .IWA3 or :3IWA;style chemicals stick;color identity;select .A:232 or .A:234 or .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:250 or .A:251 or .A:253 or .A:255 or .A:257 or .A:263 or .A:264 or .A:265 or .A:267 or .A:268 or .A:272 or .A:277 or .A:309 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:366; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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VAL232
4.282
GLY234
3.795
TYR235
3.215
LEU236
2.656
SER237
3.698
PRO238
2.984
PHE241
3.416
PHE250
4.678
HIS251
4.805
THR253
3.917
TYR255
4.772
ARG257
4.245
PHE263
3.584
TYR264
3.342
|
|||||
| Ligand Name: 8-(1~{H}-benzimidazol-2-ylmethyl)-3-cyclopropyl-7-(phenylmethyl)purine-2,6-dione | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-05-080 | PDB:7ZIJ | ||||
| Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | No | [3] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVL129 DADHPGFKDN139 VYRKRRKYFA149 DLAMNYKHGD159 PIPKVEFTEE 169 EIKTWGTVFQ179 ELNKLYPTHA189 CREYLKNLPL199 LSKYCGYRED209 NIPQLEDVSN 219 FLKERTGFSI229 RPVAGYLSPR239 DFLSGLAFRV249 FHCTQYVRHS259 SDPFYTPEPD 269 TCHELLGHVP279 LLAEPSFAQF289 SQEIGLASLG299 ASEEAVQKLA309 TCYFFTVEFG 319 LCKQDGQLRV329 FGAGLLSSIS339 ELKHALSGHA349 KVKPFDPKIT359 CKQECLITTF 369 QDVYFVSESF379 EDAKEKMREF389 TKTIK
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IVW or .IVW2 or .IVW3 or :3IVW;style chemicals stick;color identity;select .A:232 or .A:234 or .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:242 or .A:251 or .A:253 or .A:255 or .A:267 or .A:268 or .A:272 or .A:273 or .A:277 or .A:309 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:366; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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VAL232
4.352
GLY234
3.639
TYR235
3.393
LEU236
2.615
SER237
3.657
PRO238
3.041
PHE241
3.417
LEU242
4.463
HIS251
4.793
THR253
3.644
TYR255
4.122
GLU267
4.894
|
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| Ligand Name: (2~{R})-2-azanyl-3-[4-[2-azanyl-6-[(1~{R})-1-[4-chloranyl-2-(3-methylpyrazol-1-yl)phenyl]-2,2,2-tris(fluoranyl)ethoxy]pyrimidin-4-yl]phenyl]propanoic acid | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor LP533401 | PDB:7ZIK | ||||
| Method | X-ray diffraction | Resolution | 2.59 Å | Mutation | No | [3] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRVD138 NVYRKRRKYF148 ADLAMNYKHG158 DPIPKVEFTE168 EEIKTWGTVF 178 QELNKLYPTH188 ACREYLKNLP198 LLSKYCGYRE208 DNIPQLEDVS218 NFLKERTGFS 228 IRPVAGYLSP238 RDFLSGLAFR248 VFHCTQYVRH258 SSDPFYTPEP268 DTCHELLGHV 278 PLLAEPSFAQ288 FSQEIGLASL298 GASEEAVQKL308 ATCYFFTVEF318 GLCKQDGQLR 328 VFGAGLLSSI338 SELKHALSGH348 AKVKPFDPKI358 TCKQECLITT368 FQDVYFVSES 378 FEDAKEKMRE388 FTKTI
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IVN or .IVN2 or .IVN3 or :3IVN;style chemicals stick;color identity;select .A:235 or .A:236 or .A:237 or .A:238 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:272 or .A:306 or .A:309 or .A:310 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:340 or .A:364 or .A:365 or .A:366; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TYR235
3.196
LEU236
3.434
SER237
4.400
PRO238
4.001
ARG257
2.986
PHE263
4.208
TYR264
3.369
THR265
2.982
PRO266
4.344
GLU267
3.666
PRO268
3.814
HIS272
3.236
GLN306
3.300
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| Ligand Name: (3s)-8-(2-Amino-6-{(1r)-1-[5-Chloro-3'-(Methylsulfonyl)[1,1'-Biphenyl]-2-Yl]-2,2,2-Trifluoroethoxy}pyrimidin-4-Yl)-2,8-Diazaspiro[4.5]decane-3-Carboxylic Acid | Ligand Info | |||||
| Structure Description | Optimization of spirocyclic proline tryptophanhydroxylase-1 inhibitors | PDB:5TPG | ||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [1] |
| PDB Sequence |
TVPWFPKKIS
113 DLDHCNVYRK143 RRKYFADLAM153 NYKHGDPIPK163 VEFTEEEIKT173 WGTVFQELNK 183 LYPTHACREY193 LKNLPLLSKY203 CGYREDNIPQ213 LEDVSNFLKE223 RTGFSIRPVA 233 GYLSPRDFLS243 GLAFRVFHCT253 QYVRHSSDPF263 YTPEPDTCHE273 LLGHVPLLAE 283 PSFAQFSQEI293 GLASLGASEE303 AVQKLATCYF313 FTVEFGLCKQ323 DGQLRVFGAG 333 LLSSISELKH343 ALSGHAKVKP353 FDPKITCKQE363 CLITTFQDVY373 FVSESFEDAK 383 EKMREFTKTI393 K
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .7H5 or .7H52 or .7H53 or :37H5;style chemicals stick;color identity;select .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:242 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:269 or .A:272 or .A:309 or .A:310 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:364 or .A:365 or .A:366; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TYR235
3.404
LEU236
3.651
SER237
4.401
PRO238
3.280
PHE241
3.490
LEU242
3.596
ARG257
2.800
PHE263
4.498
TYR264
3.470
THR265
2.878
PRO266
3.248
GLU267
3.403
PRO268
3.559
ASP269
4.850
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|||||
| Ligand Name: Acetonitrile | Ligand Info | |||||
| Structure Description | Optimization of spirocyclic proline tryptophanhydroxylase-1 inhibitors | PDB:5TPG | ||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [1] |
| PDB Sequence |
TVPWFPKKIS
113 DLDHCNVYRK143 RRKYFADLAM153 NYKHGDPIPK163 VEFTEEEIKT173 WGTVFQELNK 183 LYPTHACREY193 LKNLPLLSKY203 CGYREDNIPQ213 LEDVSNFLKE223 RTGFSIRPVA 233 GYLSPRDFLS243 GLAFRVFHCT253 QYVRHSSDPF263 YTPEPDTCHE273 LLGHVPLLAE 283 PSFAQFSQEI293 GLASLGASEE303 AVQKLATCYF313 FTVEFGLCKQ323 DGQLRVFGAG 333 LLSSISELKH343 ALSGHAKVKP353 FDPKITCKQE363 CLITTFQDVY373 FVSESFEDAK 383 EKMREFTKTI393 K
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CCN or .CCN2 or .CCN3 or :3CCN;style chemicals stick;color identity;select .A:164 or .A:166 or .A:171 or .A:209 or .A:210 or .A:211 or .A:212 or .A:213 or .A:292 or .A:296 or .A:383 or .A:386 or .A:387 or .A:390; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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||||||
| Ligand Name: 4-[(N-{[2-(3-Methoxyphenoxy)-6-(Piperidin-1-Yl)phenyl]methyl}carbamimidoyl)carbamoyl]-L-Phenylalanine | Ligand Info | |||||
| Structure Description | Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors | PDB:5J6D | ||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [4] |
| PDB Sequence |
METVPWFPKK
111 ISDLDHCANR121 VLMYGSELDA131 DHPGFKDNVY141 RKRRKYFADL151 AMNYKHGDPI 161 PKVEFTEEEI171 KTWGTVFQEL181 NKLYPTHACR191 EYLKNLPLLS201 KYCGYREDNI 211 PQLEDVSNFL221 KERTGFSIRP231 VAGYLSPRDF241 LSGLAFRVFH251 CTQYVRHSSD 261 PFYTPEPDTC271 HELLGHVPLL281 AEPSFAQFSQ291 EIGLASLGAS301 EEAVQKLATC 311 YFFTVEFGLC321 KQDGQLRVFG331 AGLLSSISEL341 KHALSGHAKV351 KPFDPKITCK 361 QECLITTFQD371 VYFVSESFED381 AKEKMREFTK391 TI
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6H5 or .6H52 or .6H53 or :36H5;style chemicals stick;color identity;select .A:123 or .A:125 or .A:129 or .A:131 or .A:235 or .A:236 or .A:237 or .A:238 or .A:241 or .A:242 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:269 or .A:272 or .A:309 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:340 or .A:366 or .A:367; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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LEU123
4.054
TYR125
4.898
LEU129
3.831
ALA131
3.753
TYR235
2.974
LEU236
3.184
SER237
4.329
PRO238
3.835
PHE241
3.823
LEU242
3.962
ARG257
2.911
PHE263
4.632
TYR264
3.272
THR265
2.799
PRO266
3.633
|
|||||
| Ligand Name: 4-(4-amino-6-{[(1R)-1-naphthalen-2-ylethyl]amino}-1,3,5-triazin-2-yl)-L-phenylalanine | Ligand Info | |||||
| Structure Description | Crystal structure of human tryptophan hydroxylase type 1 with bound LP-521834 and FE | PDB:3HF6 | ||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [5] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCLDADH133 PGFKDNVYRK143 RRKYFADLAM153 NYKHGDPIPK163 VEFTEEEIKT 173 WGTVFRELNK183 LYPTHACREY193 LKNLPLLSKY203 CGYREDNIPQ213 LEDVSNFLKE 223 RTGFSIRPVA233 GYLSPRDFLS243 GLAFRVFHCT253 QYVRHSSDPF263 YTPEPDTCHE 273 LLGHVPLLAE283 PSFAQFSQEI293 GLASLGASEE303 AVQKLATCYF313 FTVEFGLCKQ 323 DGQLRVFGAG333 LLSSISELKH343 ALSGHAKVKP353 FDPKITCKQE363 CLITTFQDVY 373 FVSESFEDAK383 EKMREFTKTI393
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .LX0 or .LX02 or .LX03 or :3LX0;style chemicals stick;color identity;select .A:234 or .A:235 or .A:255 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:269 or .A:272 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:340 or .A:366; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
GLY234
3.541
TYR235
3.419
TYR255
3.705
ARG257
2.790
PHE263
4.551
TYR264
3.385
THR265
2.816
PRO266
3.297
GLU267
3.464
PRO268
3.483
ASP269
4.997
|
|||||
| Ligand Name: 4-{2-Amino-6-[(1r)-2,2,2-Trifluoro-1-(3'-Fluorobiphenyl-4-Yl)ethoxy]pyrimidin-4-Yl}-L-Phenylalanine | Ligand Info | |||||
| Structure Description | Crystal structure of human tryoptophan hydroxylase type 1 with bound LP-533401 and Fe | PDB:3HF8 | ||||
| Method | X-ray diffraction | Resolution | 1.85 Å | Mutation | No | [6] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRDN139 VYRKRRKYFA149 DLAMNYKHGD159 PIPKVEFTEE169 EIKTWGTVFR 179 ELNKLYPTHA189 CREYLKNLPL199 LSKYCGYRED209 NIPQLEDVSN219 FLKERTGFSI 229 RPVAGYLSPR239 DFLSGLAFRV249 FHCTQYVRHS259 SDPFYTPEPD269 TCHELLGHVP 279 LLAEPSFAQF289 SQEIGLASLG299 ASEEAVQKLA309 TCYFFTVEFG319 LCKQDGQLRV 329 FGAGLLSSIS339 ELKHALSGHA349 KVKPFDPKIT359 CKQECLITTF369 QDVYFVSESF 379 EDAKEKMREF389 TKTI
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ML0 or .ML02 or .ML03 or :3ML0;style chemicals stick;color identity;select .A:235 or .A:236 or .A:237 or .A:238 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:272 or .A:312 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:340 or .A:364 or .A:365 or .A:366; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TYR235
3.454
LEU236
3.496
SER237
3.706
PRO238
3.573
ARG257
2.752
PHE263
4.502
TYR264
3.375
THR265
2.878
PRO266
3.428
GLU267
3.449
PRO268
3.456
HIS272
3.427
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| Ligand Name: 4-(5-{[(2'-Methylbiphenyl-2-Yl)methyl]amino}pyrazin-2-Yl)-L-Phenylalanine | Ligand Info | |||||
| Structure Description | Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193 | PDB:3HFB | ||||
| Method | X-ray diffraction | Resolution | 1.92 Å | Mutation | Yes | [6] |
| PDB Sequence |
SVPWFPKKIS
113 DLDHCANRDN139 VYRKRRKYFA149 DLAMNYKHGD159 PIPKVEFTEE169 EIKTWGTVFR 179 ELNKLYPTHA189 CREYLKNLPL199 LSKYCGYRED209 NIPQLEDVSN219 FLKERTGFSI 229 RPVAGYLSPR239 DFLSGLAFRV249 FHCTQYVRHS259 SDPFYTPEPD269 TCHELLGHVP 279 LLAEPSFAQF289 SQEIGLASLG299 ASEEAVQKLA309 TCYFFTVEFG319 LCKQDGQLRV 329 FGAGLLSSIS339 ELKHALSGHA349 KVKPFDPKIT359 CKQECLITTF369 QDVYFVSESF 379 EDAKEKMREF389 TKTI
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ML4 or .ML42 or .ML43 or :3ML4;style chemicals stick;color identity;select .A:235 or .A:236 or .A:238 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:272 or .A:306 or .A:309 or .A:310 or .A:313 or .A:317 or .A:318 or .A:333 or .A:336 or .A:337 or .A:364 or .A:366; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TYR235
3.992
LEU236
4.163
PRO238
3.587
ARG257
3.000
PHE263
4.411
TYR264
3.448
THR265
2.892
PRO266
3.614
GLU267
3.746
PRO268
3.752
HIS272
3.406
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Optimization of spirocyclic proline tryptophan hydroxylase-1 inhibitors. Bioorg Med Chem Lett. 2017 Feb 1;27(3):413-419. | ||||
| REF 2 | Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry. 2002 Oct 22;41(42):12569-74. | ||||
| REF 3 | Structure-Based Design of Xanthine-Benzimidazole Derivatives as Novel and Potent Tryptophan Hydroxylase Inhibitors. J Med Chem. 2022 Aug 25;65(16):11126-11149. | ||||
| REF 4 | Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors. Bioorg Med Chem Lett. 2016 Jun 15;26(12):2855-2860. | ||||
| REF 5 | Substituted 3-(4-(1,3,5-triazin-2-yl)-phenyl)-2-aminopropanoic acids as novel tryptophan hydroxylase inhibitors. Bioorg Med Chem Lett. 2009 Sep 1;19(17):5229-32. | ||||
| REF 6 | Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis. Curr Chem Genomics. 2010 Apr 14;4:19-26. | ||||
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