Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T89458 | Target Info | |||
| Target Name | HepG2 glucose transporter (SLC2A1) | ||||
| Synonyms | Solute carrier family 2, facilitated glucose transporter member 1; HepG2 glucosetransporter; Glucose transporter type 1, erythrocyte/brain; GLUT1; GLUT-1 | ||||
| Target Type | Preclinical Target | ||||
| Gene Name | SLC2A1 | ||||
| Biochemical Class | Major facilitator | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Preverex | Ligand Info | |||||
| Structure Description | Human GLUT1 in complex with Cytochalasin B | PDB:5EQI | ||||
| Method | X-ray diffraction | Resolution | 3.00 Å | Mutation | No | [1] |
| PDB Sequence |
TGRLMLAVGG
18 AVLGSLQFGY28 NTGVINAPQK38 VIEEFYNQTW48 VHRYGESILP58 TTLTTLWSLS 68 VAIFSVGGMI78 GSFSVGLFVN88 RFGRRNSMLM98 MNLLAFVSAV108 LMGFSKLGKS 118 FEMLILGRFI128 IGVYCGLTTG138 FVPMYVGEVS148 PTALRGALGT158 LHQLGIVVGI 168 LIAQVFGLDS178 IMGNKDLWPL188 LLSIIFIPAL198 LQCIVLPFCP208 ESPRFLLINR 218 NEENRAKSVL228 KKLRGTADVT238 HDLQEMKEES248 RQMMREKKVT258 ILELFRSPAY 268 RQPILIAVVL278 QLSQQLSGIN288 AVFYYSTSIF298 EKAGVQQPVY308 ATIGSGIVNT 318 AFTVVSLFVV328 ERAGRRTLHL338 IGLAGMAGCA348 ILMTIALALL358 EQLPWMSYLS 368 IVAIFGFVAF378 FEVGPGPIPW388 FIVAELFSQG398 PRPAAIAVAG408 FSNWTSNFIV 418 GMCFQYVEQL428 CGPYVFIIFT438 VLLVLFFIFT448 YFKVPET
|
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|
|
PHE26
2.986
THR30
4.736
SER80
2.728
GLY134
4.435
THR137
2.099
GLY138
4.505
PRO141
3.068
HIS160
3.015
GLN161
2.123
ILE164
2.530
VAL165
4.188
ILE168
3.740
GLN279
4.948
GLN282
2.039
GLN283
2.669
ILE287
3.044
ASN288
2.463
PHE291
3.195
|
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| Ligand Name: B-Nonylglucoside | Ligand Info | |||||
| Structure Description | Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation | PDB:6THA | ||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [2] |
| PDB Sequence |
LTGRLMLAVG
17 GAVLGSLQFG27 YNTGVINAPQ37 KVIEEFYNQT47 WVHRYGESIL57 PTTLTTLWSL 67 SVAIFSVGGM77 IGSFSVGLFV87 NRFGRRNSML97 MMNLLAFVSA107 VLMGFSKLGK 117 SFEMLILGRF127 IIGVYCGLTT137 GFVPMYVGEV147 SPTALRGALG157 TLHQLGIVVG 167 ILIAQVFGLD177 SIMGNKDLWP187 LLLSIIFIPA197 LLQCIVLPFC207 PESPRFLLIN 217 RNEENRAKSV227 LKKLRGTADV237 THDLQEMKEE247 SRQMMREKKV257 TILELFRSPA 267 YRQPILIAVV277 LQLSQQLSGI287 NAVFYYSTSI297 FEKAGVQQPV307 YATIGSGIVN 317 TAFTVVSLFV327 VERAGRRTLH337 LIGLAGMAGC347 AILMTIALAL357 LEQLPWMSYL 367 SIVAIFGFVA377 FFEVGPGPIP387 WFIVAELFSQ397 GPRPAAIAVA407 GFSNWTSNFI 417 VGMCFQYVEQ427 LCGPYVFIIF437 TVLLVLFFIF447 TYFKVPET
|
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|
|
THR30
3.546
ARG93
3.152
ASN94
3.162
LEU97
4.234
MET98
4.160
PRO141
3.821
GLY157
4.438
HIS160
4.032
GLN161
3.295
ILE164
4.681
VAL165
3.720
ILE168
3.738
GLU209
2.574
LEU214
4.590
ARG218
2.773
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: (2~{s})-3-(4-Fluorophenyl)-2-[2-(3-Hydroxyphenyl)ethanoylamino]-~{n}-[(1~{s})-1-Phenylethyl]propanamide | Ligand Info | |||||
| Structure Description | Human GLUT1 in complex with inhibitor (2~{S})-3-(4-fluorophenyl)-2-[2-(3-hydroxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-phenylethyl]propanamide | PDB:5EQG | ||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [1] |
| PDB Sequence |
TGRLMLAVGG
18 AVLGSLQFGY28 NTGVINAPQK38 VIEEFYNQTW48 VHRYGESILP58 TTLTTLWSLS 68 VAIFSVGGMI78 GSFSVGLFVN88 RFGRRNSMLM98 MNLLAFVSAV108 LMGFSKLGKS 118 FEMLILGRFI128 IGVYCGLTTG138 FVPMYVGEVS148 PTALRGALGT158 LHQLGIVVGI 168 LIAQVFGLDS178 IMGNKDLWPL188 LLSIIFIPAL198 LQCIVLPFCP208 ESPRFLLINR 218 NEENRAKSVL228 KKLRGTADVT238 HDLQEMKEES248 RQMMREKKVT258 ILELFRSPAY 268 RQPILIAVVL278 QLSQQLSGIN288 AVFYYSTSIF298 EKAGVQQPVY308 ATIGSGIVNT 318 AFTVVSLFVV328 ERAGRRTLHL338 IGLAGMAGCA348 ILMTIALALL358 EQLPWMSYLS 368 IVAIFGFVAF378 FEVGPGPIPW388 FIVAELFSQG398 PRPAAIAVAG408 FSNWTSNFIV 418 GMCFQYVEQL428 CGPYVFIIFT438 VLLVLFFIFT448 YFKVPET
|
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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 .5RE or .5RE2 or .5RE3 or :35RE;style chemicals stick;color identity;select .A:26 or .A:30 or .A:76 or .A:80 or .A:134 or .A:137 or .A:138 or .A:141 or .A:160 or .A:161 or .A:164 or .A:168 or .A:279 or .A:282 or .A:283 or .A:287 or .A:288 or .A:291 or .A:379 or .A:380 or .A:384 or .A:388 or .A:404 or .A:405 or .A:407 or .A:408 or .A:409 or .A:411 or .A:412 or .A:415; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE26
3.182
THR30
3.584
GLY76
4.818
SER80
3.044
GLY134
4.420
THR137
1.969
GLY138
3.923
PRO141
3.915
HIS160
2.961
GLN161
2.684
ILE164
2.863
ILE168
4.250
GLN279
4.829
GLN282
2.489
GLN283
3.221
|
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| Ligand Name: (2~{s})-3-(2-Bromophenyl)-2-[2-(4-Methoxyphenyl)ethanoylamino]-~{n}-[(1~{s})-1-Phenylethyl]propanamide | Ligand Info | |||||
| Structure Description | Human GLUT1 in complex with inhibitor (2~{S})-3-(2-bromophenyl)-2-[2-(4-methoxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-phenylethyl]propanamide | PDB:5EQH | ||||
| Method | X-ray diffraction | Resolution | 2.99 Å | Mutation | No | [1] |
| PDB Sequence |
TGRLMLAVGG
18 AVLGSLQFGY28 NTGVINAPQK38 VIEEFYNQTW48 VHRYGESILP58 TTLTTLWSLS 68 VAIFSVGGMI78 GSFSVGLFVN88 RFGRRNSMLM98 MNLLAFVSAV108 LMGFSKLGKS 118 FEMLILGRFI128 IGVYCGLTTG138 FVPMYVGEVS148 PTALRGALGT158 LHQLGIVVGI 168 LIAQVFGLDS178 IMGNKDLWPL188 LLSIIFIPAL198 LQCIVLPFCP208 ESPRFLLINR 218 NEENRAKSVL228 KKLRGTADVT238 HDLQEMKEES248 RQMMREKKVT258 ILELFRSPAY 268 RQPILIAVVL278 QLSQQLSGIN288 AVFYYSTSIF298 EKAGVQQPVY308 ATIGSGIVNT 318 AFTVVSLFVV328 ERAGRRTLHL338 IGLAGMAGCA348 ILMTIALALL358 EQLPWMSYLS 368 IVAIFGFVAF378 FEVGPGPIPW388 FIVAELFSQG398 PRPAAIAVAG408 FSNWTSNFIV 418 GMCFQYVEQL428 CGPYVFIIFT438 VLLVLFFIFT448 YFKVPET
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5RF or .5RF2 or .5RF3 or :35RF;style chemicals stick;color identity;select .A:26 or .A:30 or .A:80 or .A:83 or .A:133 or .A:134 or .A:137 or .A:138 or .A:141 or .A:160 or .A:161 or .A:164 or .A:165 or .A:168 or .A:279 or .A:282 or .A:283 or .A:287 or .A:288 or .A:291 or .A:317 or .A:379 or .A:380 or .A:384 or .A:385 or .A:388 or .A:392 or .A:404 or .A:405 or .A:407 or .A:408 or .A:411 or .A:412; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE26
2.412
THR30
4.321
SER80
2.257
VAL83
4.325
CYS133
4.727
GLY134
3.864
THR137
1.783
GLY138
4.660
PRO141
3.950
HIS160
2.329
GLN161
3.254
ILE164
2.814
VAL165
4.060
ILE168
4.643
GLN279
4.289
GLN282
2.511
GLN283
3.192
|
|||||
| Ligand Name: 3,6,9,12,15,18-Hexaoxaicosane-1,20-diol | Ligand Info | |||||
| Structure Description | Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation | PDB:6THA | ||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [2] |
| PDB Sequence |
LTGRLMLAVG
17 GAVLGSLQFG27 YNTGVINAPQ37 KVIEEFYNQT47 WVHRYGESIL57 PTTLTTLWSL 67 SVAIFSVGGM77 IGSFSVGLFV87 NRFGRRNSML97 MMNLLAFVSA107 VLMGFSKLGK 117 SFEMLILGRF127 IIGVYCGLTT137 GFVPMYVGEV147 SPTALRGALG157 TLHQLGIVVG 167 ILIAQVFGLD177 SIMGNKDLWP187 LLLSIIFIPA197 LLQCIVLPFC207 PESPRFLLIN 217 RNEENRAKSV227 LKKLRGTADV237 THDLQEMKEE247 SRQMMREKKV257 TILELFRSPA 267 YRQPILIAVV277 LQLSQQLSGI287 NAVFYYSTSI297 FEKAGVQQPV307 YATIGSGIVN 317 TAFTVVSLFV327 VERAGRRTLH337 LIGLAGMAGC347 AILMTIALAL357 LEQLPWMSYL 367 SIVAIFGFVA377 FFEVGPGPIP387 WFIVAELFSQ397 GPRPAAIAVA407 GFSNWTSNFI 417 VGMCFQYVEQ427 LCGPYVFIIF437 TVLLVLFFIF447 TYFKVPET
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .P33 or .P332 or .P333 or :3P33;style chemicals stick;color identity;select .A:26 or .A:80 or .A:137 or .A:138 or .A:141 or .A:142 or .A:160 or .A:164 or .A:388 or .A:404 or .A:408 or .A:411 or .A:412; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides. Proc Natl Acad Sci U S A. 2016 Apr 26;113(17):4711-6. | ||||
| REF 2 | Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family. Life Sci Alliance. 2021 Feb 3;4(4):e202000858. | ||||
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