Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T40111 | Target Info | |||
| Target Name | Inosine-5'-monophosphate dehydrogenase 1 (IMPDH1) | ||||
| Synonyms | Superoxide-inducible protein 12; SOI12; Probable inosine-5'-monophosphate dehydrogenase IMD1; NAD-dependent inosine monophosphate dehydrogenase; Inosine dehydrogenase; IMPDH-I; IMPDH 1; IMPDH; IMPD1; IMPD 1; IMPD; IMP dehydrogenase 1; IMP dehydrogenase | ||||
| Target Type | Successful Target | ||||
| Gene Name | IMPDH1 | ||||
| Biochemical Class | CH-OH donor oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Adenosine triphosphate | Ligand Info | |||
| Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N | ||||
| InChI | 1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 | ||||
| InChIKey | ZKHQWZAMYRWXGA-KQYNXXCUSA-N | ||||
| PubChem Compound ID | 5957 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 7RFG HUMAN IMPDH1 TREATED WITH GTP, IMP, AND NAD+ OCTAMER-CENTERED | ||||||
| Method | Electron microscopy | Resolution | 2.60 Å | Mutation | No | [1] |
| PDB Sequence |
GYVPEDGLTA
20 QQLFASADGL30 TYNDFLILPG40 FIDFIADEVD50 LTSALTRKIT60 LKTPLISSPM 70 DTVTEADMAI80 AMALMGGIGF90 IHHNCTPEFQ100 ANEVRKVKKF110 EQGFITDPVV 120 LSPSHTVGDV130 LEAKMRHGFS140 GIPITETGTM150 GSKLVGIVTS160 RDIDFLAEKD 170 HTTLLSEVMT180 PRIELVVAPA190 GVTLKEANEI200 LQRSKKGKLP210 IVNDCDELVA 220 IIARTDLKKN230 RDYPLASKDS240 QKQLLCGAAV250 GTREDDKYRL260 DLLTQAGVDV 270 IVLDSSQGNS280 VYQIAMVHYI290 KQKYPHLQVI300 GGNVVTAAQA310 KNLIDAGVDG 320 LRVGMGCGSI330 CITQEVMACG340 RPQGTAVYKV350 AEYARRFGVP360 IIADGGIQTV 370 GHVVKALALG380 ASTVMMGSLL390 AATTEAPGEY400 FFSDGVRLKK410 YRGMGSLDAM 420 EKSVKIAQGV443 SGSIQDKGSI453 QKFVPYLIAG463 IQHGCQDIGA473 RSLSVLRSMM 483 YSGELKFEKR493 TMSAQIEGGV503 HGLHSYEKRL513 Y
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| PDB ID: 7RES HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+, OCTAMER-CENTERED | ||||||
| Method | Electron microscopy | Resolution | 3.05 Å | Mutation | No | [1] |
| PDB Sequence |
GGTGYVPEDG
17 LTAQQLFASA27 DGLTYNDFLI37 LPGFIDFIAD47 EVDLTSALTR57 KITLKTPLIS 67 SPMDTVTEAD77 MAIAMALMGG87 IGFIHHNCTP97 EFQANEVRKV107 KKFEQGFITD 117 PVVLSPSHTV127 GDVLEAKMRH137 GFSGIPITET147 GTLVGIVTSR161 DIDFLAEKDV 178 MTPRIELVVA188 PAGVTLKEAN198 EILQRSKKGK208 LPIVNDCDEL218 VAIIARTDLK 228 KNRDYPLASK238 DSQKQLLCGA248 AVGTREDDKY258 RLDLLTQAGV268 DVIVLDSSQG 278 NSVYQIAMVH288 YIKQKYPHLQ298 VIGGNVVTAA308 QAKNLIDAGV318 DGLRVGMGCG 328 SICITQEVMA338 CGRPQGTAVY348 KVAEYARRFG358 VPIIADGGIQ368 TVGHVVKALA 378 LGASTVMMGS388 LLAATTEAPG398 EYFFSDGVRL408 KKYRGMGSLD418 AMEKVKIAQG 442 VSGSIQDKGS452 IQKFVPYLIA462 GIQHGCQDIG472 ARSLSVLRSM482 MYSGELKFEK 492 RTMSAQIEGG502 VHGLHSYEKR512 LY
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ILE115
3.299
THR116
4.955
ASP117
4.140
PRO118
3.351
VAL119
3.015
LYS134
3.485
GLY138
4.330
PHE139
3.063
SER140
3.211
GLY141
3.157
ILE142
4.331
PRO143
3.826
ILE157
3.300
THR159
2.661
|
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| PDB ID: 7RFE HUMAN IMPDH1 TREATED WITH GTP, IMP, AND NAD+; INTERFACE-CENTERED | ||||||
| Method | Electron microscopy | Resolution | 2.60 Å | Mutation | No | [1] |
| PDB Sequence |
GYVPEDGLTA
20 QQLFASADGL30 TYNDFLILPG40 FIDFIADEVD50 LTSALTRKIT60 LKTPLISSPM 70 DTVTEADMAI80 AMALMGGIGF90 IHHNCTPEFQ100 ANEVRKVKKF110 EQGFITDPVV 120 LSPSHTVGDV130 LEAKMRHGFS140 GIPITETGTM150 GSKLVGIVTS160 RDIVMTPRIE 184 LVVAPAGVTL194 KEANEILQRS204 KKGKLPIVND214 CDELVAIIAR224 TDLKKNRDYP 234 LASKDSQKQL244 LCGAAVGTRE254 DDKYRLDLLT264 QAGVDVIVLD274 SSQGNSVYQI 284 AMVHYIKQKY294 PHLQVIGGNV304 VTAAQAKNLI314 DAGVDGLRVG324 MGCGSICITQ 334 EVMACGRPQG344 TAVYKVAEYA354 RRFGVPIIAD364 GGIQTVGHVV374 KALALGASTV 384 MMGSLLAATT394 EAPGEYFFSD404 GVRLKKYRGM414 GSLDAMKVKI439 AQGVSGSIQD 449 KGSIQKFVPY459 LIAGIQHGCQ469 DIGARSLSVL479 RSMMYSGELK489 FEKRTMSAQI 499 EGGVHGLHSY509 EKRLY
|
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|
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GLY141
4.838
ILE157
2.787
VAL158
3.407
THR159
2.298
SER160
1.689
ARG161
1.804
ASP162
1.670
MET179
4.618
THR180
1.770
GLU184
3.418
|
|||||
| PDB ID: 7RGM HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH ATP, IMP, NAD+, OCTAMER-CENTERED | ||||||
| Method | Electron microscopy | Resolution | 2.80 Å | Mutation | No | [1] |
| PDB Sequence |
GYVPEDGLTA
20 QQLFASADGL30 TYNDFLILPG40 FIDFIADEVD50 LTSALTRKIT60 LKTPLISSPM 70 DTVTEADMAI80 AMALMGGIGF90 IHHNCTPEFQ100 ANEVRKVKKF110 EQGFITDPVV 120 LSPSHTVGDV130 LEAKMRHGFS140 GIPITETGTM150 GSKLVGIVTS160 RDIDFLAEKD 170 HTTLVMTPRI183 ELVVAPAGVT193 LKEANEILQR203 SKKGKLPIVN213 DCDELVAIIA 223 RTDLKKNRDY233 PLASKDSQKQ243 LLCGAAVGTR253 EDDKYRLDLL263 TQAGVDVIVL 273 DSSQGNSVYQ283 IAMVHYIKQK293 YPHLQVIGGN303 VVTAAQAKNL313 IDAGVDGLRV 323 GMGCGSICIT333 QEVMACGRPQ343 GTAVYKVAEY353 ARRFGVPIIA363 DGGIQTVGHV 373 VKALALGAST383 VMMGSLLAAT393 TEAPGEYFFS403 DGVRLKKYRG413 MGSLDAMEKV 437 KIAQGVSGSI447 QDKGSIQKFV457 PYLIAGIQHG467 CQDIGARSLS477 VLRSMMYSGE 487 LKFEKRTMSA497 QIEGGVHGLH507 SYTF
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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 .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:115 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:134 or .A:138 or .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:157 or .A:158 or .A:159 or .A:160 or .A:161 or .A:162 or .A:180 or .A:184 or .A:185 or .A:186 or .A:187 or .A:201 or .A:205 or .A:206 or .A:207 or .A:208 or .A:209 or .A:210 or .A:221 or .A:223 or .A:224 or .A:225 or .A:226; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE115
2.784
THR116
4.227
ASP117
3.364
PRO118
2.362
VAL119
1.973
VAL120
4.504
LYS134
1.736
GLY138
3.909
PHE139
2.596
SER140
1.879
GLY141
1.946
ILE142
2.526
PRO143
2.839
ILE157
2.961
VAL158
3.417
THR159
1.713
SER160
1.755
ARG161
1.941
|
|||||
| PDB ID: 7RGQ HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH GTP, ATP, IMP, NAD+; INTERFACE-CENTERED | ||||||
| Method | Electron microscopy | Resolution | 3.90 Å | Mutation | No | [1] |
| PDB Sequence |
GYVPEDGLTA
20 QQLFASADGL30 TYNDFLILPG40 FIDFIADEVD50 LTSALTRKIT60 LKTPLISSPM 70 DTVTEADMAI80 AMALMGGIGF90 IHHNCTPEFQ100 ANEVRKVKKF110 EQGFITDPVV 120 LSPSHTVGDV130 LEAKMRHGFS140 GIPITETGTM150 GSKLVGIVTS160 RDIDFDHTTL 174 LSEVMTPRIE184 LVVAPAGVTL194 KEANEILQRS204 KKGKLPIVND214 CDELVAIIAR 224 TDLKKNRDYP234 LASKDSQKQL244 LCGAAVGTRE254 DDKYRLDLLT264 QAGVDVIVLD 274 SSQGNSVYQI284 AMVHYIKQKY294 PHLQVIGGNV304 VTAAQAKNLI314 DAGVDGLRVG 324 MGCGSICITQ334 EVMACGRPQG344 TAVYKVAEYA354 RRFGVPIIAD364 GGIQTVGHVV 374 KALALGASTV384 MMGSLLAATT394 EAPGEYFFSD404 GVRLKKYRGM414 GSLKIAQGVS 444 GSIQDKGSIQ454 KFVPYLIAGI464 QHGCQDIGAR474 SLSVLRSMMY484 SGELKFEKRT 494 MSAQIEGGVH504 GLHSYTFLPF514 T
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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 .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:140 or .A:141 or .A:157 or .A:158 or .A:159 or .A:160 or .A:161 or .A:162 or .A:179 or .A:180 or .A:184 or .A:185 or .A:186 or .A:187 or .A:206 or .A:207 or .A:208 or .A:209 or .A:210; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| PDB ID: 7RFH HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH ATP, OCTAMER-CENTERED | ||||||
| Method | Electron microscopy | Resolution | 3.70 Å | Mutation | No | [1] |
| PDB Sequence |
HETAAQRYSA
-11 RLLQAGYMAD3 YLISGGTGYV13 PEDGLTAQQL23 FASADGLTYN33 DFLILPGFID 43 FIADEVDLTS53 ALTRKITLKT63 PLISSPMDTV73 TEADMAIAMA83 LMGGIGFIHH 93 NCTPEFQANE103 VRKVKKFEQG113 FITDPVVLSP123 SHTVGDVLEA133 KMRHGFSGIP 143 ITETGTLVGI157 VTSRDIDFLL174 LSEVMTPRIE184 LVVAPAGVTL194 KEANEILQRS 204 KKGKLPIVND214 CDELVAIIAR224 TDLKKNRDYP234 LASKDSQKQL244 LCGAAVGTRE 254 DDKYRLDLLT264 QAGVDVIVLD274 SSQGNSVYQI284 AMVHYIKQKY294 PHLQVIGGNV 304 VTAAQAKNLI314 DAGVDGLRVG324 MGCVMACGRP342 QGTAVYKVAE352 YARRFGVPII 362 ADGGIQTVGH372 VVKALALGAS382 TVMMGSLLAA392 TTEAPGSIQK455 FVPYLIAGIQ 465 HGCQDIGARS475 LSVLRSMMYS485 GELKFEKRTM495 SAQIEGGVH
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:115 or .A:117 or .A:118 or .A:119 or .A:120 or .A:134 or .A:138 or .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:157 or .A:158 or .A:159 or .A:160 or .A:161 or .A:162 or .A:180 or .A:183 or .A:184 or .A:185 or .A:186 or .A:187 or .A:204 or .A:206 or .A:207 or .A:208 or .A:209 or .A:210 or .A:221 or .A:223 or .A:225 or .A:226; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE115
2.203
ASP117
3.698
PRO118
2.634
VAL119
1.936
VAL120
4.451
LYS134
1.924
GLY138
4.143
PHE139
2.239
SER140
2.218
GLY141
1.819
ILE142
3.358
PRO143
2.665
ILE157
2.952
VAL158
3.445
THR159
2.280
SER160
2.393
ARG161
1.794
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | IMPDH1 retinal variants control filament architecture to tune allosteric regulation. Nat Struct Mol Biol. 2022 Jan;29(1):47-58. | ||||
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