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 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
DGAT1_HUMAN
Ligand General Information  Top
Ligand Name 1-Hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine Ligand Info
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)([O-])OCC[NH3+])OC(=O)CCCCCCCC=CCCCCCCCC
InChI 1S/C39H76NO8P/c1-3-5-7-9-11-13-15-17-18-20-22-24-26-28-30-32-39(42)48-37(36-47-49(43,44)46-34-33-40)35-45-38(41)31-29-27-25-23-21-19-16-14-12-10-8-6-4-2/h17-18,37H,3-16,19-36,40H2,1-2H3,(H,43,44)/b18-17-/t37-/m1/s1
InChIKey FHQVHHIBKUMWTI-OTMQOFQLSA-N
PubChem Compound ID 59834030
Drug Binding Sites of Target  Top
PDB ID: 6VYI      Cryo-EM structure of human diacylglycerol O-acyltransferase 1
Method Electron microscopy Resolution 3.00 Å Mutation No [1]
PDB Sequence
LRCHRLQDSL
75
FSSDSGFSNY
85
RGILNWCVVM
95
LILSNARLFL
105
ENLIKYGILV
115

DPIQVVSLFL
125
KDPYSWPAPC
135
LVIAANVFAV
145
AAFQVEKRLA
155
VGALTEQAGL
165

LLHVANLATI
175
LCFPAAVVLL
185
VESITPVGSL
195
LALMAHTILF
205
LKLFSYRDVN
215

SWCRRARAKA
225
ASAHTVSYPD
245
NLTYRDLYYF
255
LFAPTLCYEL
265
NFPRSPRIRK
275

RFLLRRILEM
285
LFFTQLQVGL
295
IQQWMVPTIQ
305
NSMKPFKDMD
315
YSRIIERLLK
325

LAVPNHLIWL
335
IFFYWLFHSC
345
LNAVAELMQF
355
GDREFYRDWW
365
NSESVTYFWQ
375

NWNIPVHKWC
385
IRHFYKPMLR
395
RGSSKWMART
405
GVFLASAFFH
415
EYLVSVPLRM
425

FRLWAFTGMM
435
AQIPLAWFVG
445
RFFQGNYGNA
455
AVWLSLIIGQ
465
PIAVLMYVHD
475

YYVLNY
Residue
Distance (Å)
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
Residue
Distance (Å)
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
PDB ID: 6VZ1      Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate
Method Electron microscopy Resolution 3.20 Å Mutation No [1]
PDB Sequence
WELRCHRLQD
73
SLFSSDSGFS
83
NYRGILNWCV
93
VMLILSNARL
103
FLENLIKYGI
113

LVDPIQVVSL
123
FLKDPYSWPA
133
PCLVIAANVF
143
AVAAFQVEKR
153
LAVGALTEQA
163

GLLLHVANLA
173
TILCFPAAVV
183
LLVESITPVG
193
SLLALMAHTI
203
LFLKLFSYRD
213

VNSWCRRARA
223
KAASAAAPHT
240
VSYPDNLTYR
250
DLYYFLFAPT
260
LCYELNFPRS
270

PRIRKRFLLR
280
RILEMLFFTQ
290
LQVGLIQQWM
300
VPTIQNSMKP
310
FKDMDYSRII
320

ERLLKLAVPN
330
HLIWLIFFYW
340
LFHSCLNAVA
350
ELMQFGDREF
360
YRDWWNSESV
370

TYFWQNWNIP
380
VHKWCIRHFY
390
KPMLRRGSSK
400
WMARTGVFLA
410
SAFFHEYLVS
420

VPLRMFRLWA
430
FTGMMAQIPL
440
AWFVGRFFQG
450
NYGNAAVWLS
460
LIIGQPIAVL
470

MYVHDYYVLN
480
Y
Residue
Distance (Å)
PHE76
3.811
SER77
4.194
SER78
1.372
ARG86
3.521
LEU89
3.481
ASN90
4.849
TRP91
4.022
CYS92
3.308
VAL93
3.245
MET95
3.787
LEU96
3.901
SER99
3.236
ASN100
3.547
LEU103
4.764
GLU284
4.714
PHE288
3.035
Residue
Distance (Å)
LEU291
3.559
LEU295
4.049
GLN298
4.787
LEU324
4.143
LEU332
3.773
LEU335
3.595
ILE336
3.655
PHE338
3.309
TYR339
3.068
TRP364
3.588
TRP365
4.680
ASN451
3.720
TYR452
3.498
ALA455
3.600
TRP458
4.198
LEU459
4.050
References  Top
REF 1 Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme. Nature. 2020 May;581(7808):323-328.

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