Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T16688 | Target Info | |||
| Target Name | Diacylglycerol acyltransferase 1 (DGAT1) | ||||
| Synonyms | Retinol O-fatty-acyltransferase; Diglyceride acyltransferase; Diacylglycerol O-acyltransferase 1; DGAT; Acyl-CoA retinol O-fatty-acyltransferase; ARAT; AGRP1; ACAT-related gene product 1 | ||||
| Target Type | Successful Target | ||||
| Gene Name | DGAT1 | ||||
| Biochemical Class | Acyltransferase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Oleoyl-CoA | Ligand Info | |||||
| Structure Description | Human Diacylglycerol Acyltransferase 1 in complex with oleoyl-CoA | PDB:6VP0 | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | No | [1] |
| PDB Sequence |
WELRCHRLQD
73 SLFSSDSGFS83 NYRGILNWCV93 VMLILSNARL103 FLENLIKYGI113 LVDPIQVVSL 123 FLKDPYSWPA133 PCLVIAANVF143 AVAAFQVEKR153 LAVGALTEQA163 GLLLHVANLA 173 TILCFPAAVV183 LLVESITPVG193 SLLALMAHTI203 LFLKLFSYRD213 VNSWCRRARA 223 KHTVSYPDNL247 TYRDLYYFLF257 APTLCYELNF267 PRSPRIRKRF277 LLRRILEMLF 287 FTQLQVGLIQ297 QWMVPTIQNS307 MKPFKDMDYS317 RIIERLLKLA327 VPNHLIWLIF 337 FYWLFHSCLN347 AVAELMQFGD357 REFYRDWWNS367 ESVTYFWQNW377 NIPVHKWCIR 387 HFYKPMLRRG397 SSKWMARTGV407 FLASAFFHEY417 LVSVPLRMFR427 LWAFTGMMAQ 437 IPLAWFVGRF447 FQGNYGNAAV457 WLSLIIGQPI467 AVLMYVHDYY477 VLNY |
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|
|
MET199
4.281
TRP334
3.516
LEU335
4.384
PHE337
4.208
PHE338
3.339
LEU341
4.233
PHE342
4.147
TRP364
3.973
THR371
3.839
PHE373
3.748
TRP374
2.875
GLN375
3.167
TRP377
2.429
ASN378
4.031
VAL381
4.024
HIS382
2.339
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Phosphatidylserine | Ligand Info | |||||
| Structure Description | Human Diacylglycerol Acyltransferase 1 in complex with oleoyl-CoA | PDB:6VP0 | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | No | [1] |
| PDB Sequence |
WELRCHRLQD
73 SLFSSDSGFS83 NYRGILNWCV93 VMLILSNARL103 FLENLIKYGI113 LVDPIQVVSL 123 FLKDPYSWPA133 PCLVIAANVF143 AVAAFQVEKR153 LAVGALTEQA163 GLLLHVANLA 173 TILCFPAAVV183 LLVESITPVG193 SLLALMAHTI203 LFLKLFSYRD213 VNSWCRRARA 223 KHTVSYPDNL247 TYRDLYYFLF257 APTLCYELNF267 PRSPRIRKRF277 LLRRILEMLF 287 FTQLQVGLIQ297 QWMVPTIQNS307 MKPFKDMDYS317 RIIERLLKLA327 VPNHLIWLIF 337 FYWLFHSCLN347 AVAELMQFGD357 REFYRDWWNS367 ESVTYFWQNW377 NIPVHKWCIR 387 HFYKPMLRRG397 SSKWMARTGV407 FLASAFFHEY417 LVSVPLRMFR427 LWAFTGMMAQ 437 IPLAWFVGRF447 FQGNYGNAAV457 WLSLIIGQPI467 AVLMYVHDYY477 VLNY |
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|
|
TRP299
3.833
PHE311
4.179
LYS312
4.162
ASP313
3.849
MET314
2.842
ASP315
4.924
TYR316
3.387
ILE319
4.050
ILE320
4.480
LEU323
4.217
LEU324
3.144
LYS325
3.412
ALA327
3.894
|
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| Ligand Name: 1-Hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine | Ligand Info | |||||
| Structure Description | Cryo-EM structure of human diacylglycerol O-acyltransferase 1 | PDB:6VYI | ||||
| Method | Electron microscopy | Resolution | 3.00 Å | Mutation | No | [2] |
| PDB Sequence |
LRCHRLQDSL
75 FSSDSGFSNY85 RGILNWCVVM95 LILSNARLFL105 ENLIKYGILV115 DPIQVVSLFL 125 KDPYSWPAPC135 LVIAANVFAV145 AAFQVEKRLA155 VGALTEQAGL165 LLHVANLATI 175 LCFPAAVVLL185 VESITPVGSL195 LALMAHTILF205 LKLFSYRDVN215 SWCRRARAKA 225 ASAHTVSYPD245 NLTYRDLYYF255 LFAPTLCYEL265 NFPRSPRIRK275 RFLLRRILEM 285 LFFTQLQVGL295 IQQWMVPTIQ305 NSMKPFKDMD315 YSRIIERLLK325 LAVPNHLIWL 335 IFFYWLFHSC345 LNAVAELMQF355 GDREFYRDWW365 NSESVTYFWQ375 NWNIPVHKWC 385 IRHFYKPMLR395 RGSSKWMART405 GVFLASAFFH415 EYLVSVPLRM425 FRLWAFTGMM 435 AQIPLAWFVG445 RFFQGNYGNA455 AVWLSLIIGQ465 PIAVLMYVHD475 YYVLNY |
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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 .6OU or .6OU2 or .6OU3 or :36OU;style chemicals stick;color identity;select .A:76 or .A:77 or .A:78 or .A:79 or .A:86 or .A:89 or .A:90 or .A:91 or .A:92 or .A:93 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:102 or .A:104 or .A:105 or .A:277 or .A:280 or .A:281 or .A:283 or .A:284 or .A:287 or .A:288 or .A:291 or .A:295 or .A:299 or .A:324 or .A:332 or .A:335 or .A:336 or .A:338 or .A:339 or .A:343 or .A:364 or .A:365 or .A:451 or .A:452 or .A:455 or .A:458 or .A:459; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE76
2.746
SER77
4.034
SER78
2.482
ASP79
4.602
ARG86
2.959
LEU89
3.185
ASN90
3.516
TRP91
4.113
CYS92
3.497
VAL93
3.053
VAL94
4.293
MET95
3.552
LEU96
3.599
ILE97
3.593
LEU98
3.744
SER99
3.471
ASN100
3.324
ALA101
3.749
ARG102
4.568
PHE104
3.985
LEU105
3.661
PHE277
3.954
ARG280
3.318
ARG281
3.297
LEU283
4.498
GLU284
3.106
PHE287
3.679
PHE288
3.210
LEU291
4.555
LEU295
3.706
TRP299
4.568
LEU324
4.250
LEU332
3.818
LEU335
3.203
ILE336
3.825
PHE338
3.511
TYR339
3.052
HIS343
4.515
TRP364
4.379
TRP365
4.818
ASN451
3.808
TYR452
2.556
ALA455
3.516
TRP458
4.131
LEU459
3.841
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Lauryl Maltose Neopentyl Glycol | Ligand Info | |||||
| Structure Description | Human Diacylglycerol Acyltransferase 1 in complex with oleoyl-CoA | PDB:6VP0 | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | No | [1] |
| PDB Sequence |
WELRCHRLQD
73 SLFSSDSGFS83 NYRGILNWCV93 VMLILSNARL103 FLENLIKYGI113 LVDPIQVVSL 123 FLKDPYSWPA133 PCLVIAANVF143 AVAAFQVEKR153 LAVGALTEQA163 GLLLHVANLA 173 TILCFPAAVV183 LLVESITPVG193 SLLALMAHTI203 LFLKLFSYRD213 VNSWCRRARA 223 KHTVSYPDNL247 TYRDLYYFLF257 APTLCYELNF267 PRSPRIRKRF277 LLRRILEMLF 287 FTQLQVGLIQ297 QWMVPTIQNS307 MKPFKDMDYS317 RIIERLLKLA327 VPNHLIWLIF 337 FYWLFHSCLN347 AVAELMQFGD357 REFYRDWWNS367 ESVTYFWQNW377 NIPVHKWCIR 387 HFYKPMLRRG397 SSKWMARTGV407 FLASAFFHEY417 LVSVPLRMFR427 LWAFTGMMAQ 437 IPLAWFVGRF447 FQGNYGNAAV457 WLSLIIGQPI467 AVLMYVHDYY477 VLNY |
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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 .AV0 or .AV02 or .AV03 or :3AV0;style chemicals stick;color identity;select .C:100 or .C:103 or .C:104 or .C:287 or .C:290 or .C:291 or .C:294 or .C:295 or .C:298 or .C:299 or .C:303 or .C:332; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure and mechanism of human diacylglycerol O-acyltransferase?1. Nature. 2020 May;581(7808):329-332. | ||||
| REF 2 | Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme. Nature. 2020 May;581(7808):323-328. | ||||
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