Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T86573 Target Info
Target Name HUMAN inosine-5'-monophosphate dehydrogenase 2 (IMPDH2)
Synonyms IMPDH-II; IMPDH 2; IMPD2; IMPD 2; IMP dehydrogenase 2
Gene Name IMPDH2
Biochemical Class CH-OH donor oxidoreductase
UniProt ID
IMDH2_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Adenosine triphosphate Ligand Info
Structure Description Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Fully compressed filament segment reconstruction. PDB:6UDO
Method Electron microscopy Resolution 3.21 Å Mutation No [1]
PDB Sequence
YVPDDGLTAQ
21
QLFNCGDGLT
31
YNDFLILPGY
41
IDFTADQVDL
51
TSALTKKITL
61

KTPLVSSPMD
71
TVTEAGMAIA
81
MALTGGIGFI
91
HHNCTPEFQA
101
NEVRKVKKYE
111

QGFITDPVVL
121
SPKDRVRDVF
131
EAKARHGFCG
141
IPITDTGRMG
151
SRLVGIISSR
161

DIDFLKEEEH
171
DCFLEEIMTK
181
REDLVVAPAG
191
ITLKEANEIL
201
QRSKKGKLPI
211

VNEDDELVAI
221
IARTDLKKNR
231
DYPLASKDAK
241
KQLLCGAAIG
251
THEDDKYRLD
261

LLAQAGVDVV
271
VLDSSQGNSI
281
FQINMIKYIK
291
DKYPNLQVIG
301
GNVVTAAQAK
311

NLIDAGVDAL
321
RVGMGSGSIC
331
ITQEVLACGR
341
PQATAVYKVS
351
EYARRFGVPV
361

IADGGIQNVG
371
HIAKALALGA
381
STVMMGSLLA
391
ATTEAPGEYF
401
FSDGIRLKKY
411

RGMGSLDAMI
437
KVAQGVSGAV
447
QDKGSIHKFV
457
PYLIAGIQHS
467
CQDIGAKSLT
477

QVRAMMYSGE
487
LKFEKRTSSA
497
QVEGGVHSLH
507
SYEKRLF
Residue
Distance (Å)
ILE157
3.843
SER159
2.300
SER160
2.786
ARG161
2.680
ASP162
3.106
ASP164
4.802
THR180
3.013
ASP184
4.016
Residue
Distance (Å)
LEU185
3.431
VAL186
3.354
LYS206
3.360
GLY207
3.231
LYS208
2.461
LEU209
3.841
PRO210
3.792
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: C2-MAD Ligand Info
Structure Description Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with Ribavirin Monophosphate and C2-Mycophenolic Adenine Dinucleotide PDB:1NF7
Method X-ray diffraction Resolution 2.65 Å Mutation No [2]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

YEQGFITDPV
119
VLSPKGIISS
160
RDIDFLEHDC
173
FLEEIMTKRE
183
DLVVAPAGIT
193

LKEANEILQR
203
SKKGKLPIVN
213
EDDELVAIIA
223
RTLKKNRDYP
234
LASKDAKKQL
244

LCGAAIGTHE
254
DDKYRLDLLA
264
QAGVDVVVLD
274
SSQGNSIFQI
284
NMIKYIKDKY
294

PNLQVIGGNV
304
VTAAQAKNLI
314
DAGVDALRVG
324
MGSGSICITQ
334
EVLACGRPQA
344

TAVYKVSEYA
354
RRFGVPVIAD
364
GGIQNVGHIA
374
KALALGASTV
384
MMGSLLAATT
394

EAPGEYFFSD
404
GIRLKKYRGM
414
GSLDAMIKVA
440
QGVSGAVQDK
450
GSIHKFVPYL
460

IAGIQHSCQD
470
IGAKSLTQVR
480
AMMYSGELKF
490
EKRTSSAQVE
500
GGVHSLHSYE
510

KRLF
Residue
Distance (Å)
THR252
3.503
HIS253
3.519
GLU254
4.484
ASP274
3.444
SER275
3.211
SER276
2.456
GLN277
4.852
PHE282
2.967
ASN303
3.172
ARG322
3.455
Residue
Distance (Å)
GLY324
3.385
MET325
3.417
GLY326
3.273
CYS331
2.836
THR333
2.861
ASP364
4.944
MET414
4.896
GLY415
3.889
GLN441
3.075
Ligand Name: 6-Chloropurine Riboside, 5'-Monophosphate Ligand Info
Structure Description TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE PDB:1B3O
Method X-ray diffraction Resolution 2.90 Å Mutation No [3]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

DYPLASKDAK
241
KQLLCGAAIG
251
THEDDKYRLD
261
LLAQAGVDVV
271
VLDSSQGNSI
281

FQINMIKYIK
291
DKYPNLQVIG
301
GNVVTAAQAK
311
NLIDAGVDAL
321
RVGMGSRPQA
344

TAVYKVSEYA
354
RRFGVPVIAD
364
GGIQNVGHIA
374
KALALGASTV
384
MMGSLLAATT
394

EAPGEYDKGS
452
IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492

RTSSAQV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CPR or .CPR2 or .CPR3 or :3CPR;style chemicals stick;color identity;select .A:68 or .A:69 or .A:70 or .A:303 or .A:322 or .A:327 or .A:364 or .A:365 or .A:366 or .A:367 or .A:385 or .A:386 or .A:387 or .A:388 or .A:389; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.126
PRO69
4.689
MET70
3.748
ASN303
3.834
ARG322
2.796
SER327
3.693
ASP364
2.477
GLY365
3.800
Residue
Distance (Å)
GLY366
2.972
ILE367
4.621
MET385
3.567
MET386
3.940
GLY387
2.957
SER388
2.420
LEU389
4.769
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Nicotinamide-Adenine-Dinucleotide Ligand Info
Structure Description Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with 6Cl-IMP and NAD PDB:1NFB
Method X-ray diffraction Resolution 2.90 Å Mutation No [4]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

YEQGFITDPV
119
VLSPGIPITD
146
TGRMGSAPAG
191
ITLKEANEIL
201
QRSKKGKLPI
211

VNEDDEVAII
222
ANRDYPLASK
238
DAKKQLLCGA
248
AIGTHEDDKY
258
RLDLLAQAGV
268

DVVVLDSSQG
278
NSIFQINMIK
288
YIKDKYPNLQ
298
VIGGNVVTAA
308
QAKNLIDAGV
318

DALRVGMGSG
328
SICITQEVLA
338
CGRPQATAVY
348
KVSEYARRFG
358
VPVIADGGIQ
368

NVGHIAKALA
378
LGASTVMMGS
388
LLAATTEAPG
398
EYFFSDGIRL
408
KKYRGMDKGS
452

IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492
RTSSAQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:93 or .A:252 or .A:253 or .A:254 or .A:274 or .A:275 or .A:276 or .A:277 or .A:282 or .A:303 or .A:322 or .A:333 or .A:335 or .A:364 or .A:414; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
HIS93
4.755
THR252
3.274
HIS253
3.008
GLU254
4.011
ASP274
2.609
SER275
2.455
SER276
2.699
GLN277
4.513
Residue
Distance (Å)
PHE282
3.451
ASN303
3.545
ARG322
2.839
THR333
4.854
GLU335
4.219
ASP364
4.261
MET414
4.645
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Selenazole-4-Carboxyamide-Adenine Dinucleotide Ligand Info
Structure Description TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE PDB:1B3O
Method X-ray diffraction Resolution 2.90 Å Mutation No [3]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

DYPLASKDAK
241
KQLLCGAAIG
251
THEDDKYRLD
261
LLAQAGVDVV
271
VLDSSQGNSI
281

FQINMIKYIK
291
DKYPNLQVIG
301
GNVVTAAQAK
311
NLIDAGVDAL
321
RVGMGSRPQA
344

TAVYKVSEYA
354
RRFGVPVIAD
364
GGIQNVGHIA
374
KALALGASTV
384
MMGSLLAATT
394

EAPGEYDKGS
452
IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492

RTSSAQV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SAE or .SAE2 or .SAE3 or :3SAE;style chemicals stick;color identity;select .A:93 or .A:252 or .A:253 or .A:254 or .A:274 or .A:275 or .A:276 or .A:277 or .A:282 or .A:303 or .A:322 or .A:324 or .A:325 or .A:364; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
HIS93
3.973
THR252
3.435
HIS253
3.275
GLU254
4.632
ASP274
2.335
SER275
3.246
SER276
2.841
Residue
Distance (Å)
GLN277
4.660
PHE282
3.094
ASN303
2.834
ARG322
4.248
GLY324
3.351
MET325
4.441
ASP364
3.764
Ligand Name: Guanosine-5'-Diphosphate Ligand Info
Structure Description Structure of human IMP dehydrogenase, isoform 2, bound to GDP PDB:6I0M
Method X-ray diffraction Resolution 2.57 Å Mutation No [5]
PDB Sequence
YVPDDGLTAQ
21
QLFNCGDGLT
31
YNDFLILPGY
41
IDFTADQVDL
51
TSALTKKITL
61

KTPLVSSPMD
71
TVTEAGMAIA
81
MALTGGIGFI
91
HHNCTPEFQA
101
NEVRKVKKYE
111

QGFITDPVVL
121
SPKDRVRDVF
131
EAKARHGFCG
141
IPITDTGRMG
151
SRLVGIISSR
161

DIDFLEHDCF
174
LEEIMTKRED
184
LVVAPAGITL
194
KEANEILQRS
204
KKGKLPIVNE
214

DDELVAIIAR
224
TDLKKNRDYP
234
LASKDAKKQL
244
LCGAAIGTHE
254
DDKYRLDLLA
264

QAGVDVVVLD
274
SSQGNSIFQI
284
NMIKYIKDKY
294
PNLQVIGGNV
304
VTAAQAKNLI
314

DAGVDALRVG
324
MGSGSITQEV
336
LACGRPQATA
346
VYKVSEYARR
356
FGVPVIADGG
366

IQNVGHIAKA
376
LALGASTVMM
386
GSLLAATTEA
396
PGEYFFSDGM
414
GSLDAQDKGS
452

IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492
RTSSAQVEGG
502
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:109 or .A:110 or .A:111 or .A:112 or .A:113 or .A:115 or .A:117 or .A:118 or .A:119 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:179 or .A:180 or .A:184 or .A:185 or .A:186 or .A:194 or .A:195 or .A:198 or .A:204 or .A:206 or .A:207 or .A:208 or .A:209 or .A:210 or .A:221 or .A:222 or .A:223 or .A:225 or .A:226 or .A:227 or .A:229 or .A:230 or .A:238 or .A:242; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS109
2.112
TYR110
2.619
GLU111
2.459
GLN112
1.927
GLY113
2.809
ILE115
2.600
ASP117
4.481
PRO118
2.574
VAL119
2.550
GLY138
4.946
PHE139
2.297
CYS140
1.813
GLY141
2.251
ILE142
4.382
PRO143
4.884
ILE157
2.974
ILE158
3.535
SER159
1.810
SER160
2.652
ARG161
2.337
ASP162
1.949
MET179
4.483
THR180
1.885
Residue
Distance (Å)
ASP184
2.168
LEU185
1.578
VAL186
1.357
LEU194
2.712
LYS195
2.784
ASN198
1.993
SER204
4.992
LYS206
2.390
GLY207
1.911
LYS208
1.540
LEU209
4.051
PRO210
3.519
ILE221
3.734
ILE222
3.333
ALA223
2.434
THR225
2.336
ASP226
1.604
LEU227
2.955
LYS229
2.418
ASN230
2.991
LYS238
2.698
LYS242
2.277
Ligand Name: Guanosine-5'-Monophosphate Ligand Info
Structure Description Structure of human IMP dehydrogenase, isoform 2, bound to GDP PDB:6I0M
Method X-ray diffraction Resolution 2.57 Å Mutation No [5]
PDB Sequence
YVPDDGLTAQ
21
QLFNCGDGLT
31
YNDFLILPGY
41
IDFTADQVDL
51
TSALTKKITL
61

KTPLVSSPMD
71
TVTEAGMAIA
81
MALTGGIGFI
91
HHNCTPEFQA
101
NEVRKVKKYE
111

QGFITDPVVL
121
SPKDRVRDVF
131
EAKARHGFCG
141
IPITDTGRMG
151
SRLVGIISSR
161

DIDFLEHDCF
174
LEEIMTKRED
184
LVVAPAGITL
194
KEANEILQRS
204
KKGKLPIVNE
214

DDELVAIIAR
224
TDLKKNRDYP
234
LASKDAKKQL
244
LCGAAIGTHE
254
DDKYRLDLLA
264

QAGVDVVVLD
274
SSQGNSIFQI
284
NMIKYIKDKY
294
PNLQVIGGNV
304
VTAAQAKNLI
314

DAGVDALRVG
324
MGSGSITQEV
336
LACGRPQATA
346
VYKVSEYARR
356
FGVPVIADGG
366

IQNVGHIAKA
376
LALGASTVMM
386
GSLLAATTEA
396
PGEYFFSDGM
414
GSLDAQDKGS
452

IHKFVPYLIA
462
GIQHSCQDIG
472
AKSLTQVRAM
482
MYSGELKFEK
492
RTSSAQVEGG
502
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5GP or .5GP2 or .5GP3 or :35GP;style chemicals stick;color identity;select .A:68 or .A:69 or .A:70 or .A:274 or .A:276 or .A:303 or .A:322 or .A:325 or .A:326 or .A:327 or .A:328 or .A:329 or .A:332 or .A:333 or .A:364 or .A:365 or .A:366 or .A:367 or .A:385 or .A:386 or .A:387 or .A:388 or .A:389 or .A:414 or .A:415 or .A:416; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
1.649
PRO69
3.617
MET70
2.488
ASP274
4.601
SER276
3.967
ASN303
3.984
ARG322
1.270
MET325
4.630
GLY326
3.536
SER327
3.868
GLY328
2.561
SER329
3.830
ILE332
4.669
Residue
Distance (Å)
THR333
1.907
ASP364
1.641
GLY365
2.760
GLY366
2.818
ILE367
3.632
MET385
3.672
MET386
3.723
GLY387
2.823
SER388
1.756
LEU389
4.288
MET414
3.273
GLY415
2.361
SER416
4.197
Ligand Name: Guanosine-5'-Triphosphate Ligand Info
Structure Description Structure of human IMP dehydrogenase, isoform 2, bound to GTP PDB:6I0O
Method X-ray diffraction Resolution 2.62 Å Mutation No [5]
PDB Sequence
SYVPDDGLTA
20
QQLFNCGDGL
30
TYNDFLILPG
40
YIDFTADQVD
50
LTSALTKKIT
60

LKTPLVSSPM
70
DTVTEAGMAI
80
AMALTGGIGF
90
IHHNCTPEFQ
100
ANEVRKVKKY
110

EQGFITDPVV
120
LSPKDRVRDV
130
FEAKARHGFC
140
GIPITDTGRM
150
GSRLVGIISS
160

RDIDFLKEEE
170
HDCFLEEIMT
180
KREDLVVAPA
190
GITLKEANEI
200
LQRSKKGKLP
210

IVNEDDELVA
220
IIARTDLKKN
230
RDYPLASKDA
240
KKQLLCGAAI
250
GTHEDDKYRL
260

DLLAQAGVDV
270
VVLDSSQGNS
280
IFQINMIKYI
290
KDKYPNLQVI
300
GGNVVTAAQA
310

KNLIDAGVDA
320
LRVGMEVLAC
339
GRPQATAVYK
349
VSEYARRFGV
359
PVIADGGIQN
369

VGHIAKALAL
379
GASTVMMGSL
389
LAATTEAPGE
399
YFFSKGSIHK
455
FVPYLIAGIQ
465

HSCQDIGAKS
475
LTQVRAMMYS
485
GELKFEKRTS
495
SAQV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GTP or .GTP2 or .GTP3 or :3GTP;style chemicals stick;color identity;select .A:62 or .A:109 or .A:110 or .A:111 or .A:112 or .A:113 or .A:114 or .A:115 or .A:117 or .A:118 or .A:119 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:179 or .A:180 or .A:184 or .A:185 or .A:186 or .A:194 or .A:195 or .A:198 or .A:202 or .A:205 or .A:206 or .A:207 or .A:208 or .A:209 or .A:210 or .A:221 or .A:222 or .A:223 or .A:225 or .A:226 or .A:227 or .A:229 or .A:230 or .A:233 or .A:234 or .A:235 or .A:236 or .A:238 or .A:242; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS62
3.301
LYS109
2.515
TYR110
2.871
GLU111
2.492
GLN112
2.152
GLY113
2.417
PHE114
4.834
ILE115
2.695
ASP117
4.479
PRO118
2.494
VAL119
2.638
LYS134
3.398
GLY138
3.914
PHE139
2.549
CYS140
2.125
GLY141
1.583
ILE142
3.585
PRO143
4.107
ILE157
2.242
ILE158
3.235
SER159
1.842
SER160
1.606
ARG161
2.424
ASP162
2.319
MET179
4.979
THR180
2.461
ASP184
2.620
Residue
Distance (Å)
LEU185
2.488
VAL186
1.843
LEU194
2.622
LYS195
3.764
ASN198
1.962
GLN202
4.486
LYS205
4.572
LYS206
2.699
GLY207
1.740
LYS208
2.007
LEU209
3.904
PRO210
3.456
ILE221
3.620
ILE222
3.374
ALA223
3.603
THR225
2.173
ASP226
1.908
LEU227
3.072
LYS229
1.710
ASN230
1.675
TYR233
3.054
PRO234
2.756
LEU235
4.212
ALA236
3.653
LYS238
1.785
LYS242
2.196
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Inosinic Acid Ligand Info
Structure Description Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Filament assembly interface reconstruction. PDB:6UDP
Method Electron microscopy Resolution 2.95 Å Mutation No [1]
PDB Sequence
MADYLISGGT
10
SYVPDDGLTA
20
QQLFNCGDGL
30
TYNDFLILPG
40
YIDFTADQVD
50

LTSALTKKIT
60
LKTPLVSSPM
70
DTVTEAGMAI
80
AMALTGGIGF
90
IHHNCTPEFQ
100

ANEVRKVKKY
110
YPLASKDAKK
242
QLLCGAAIGT
252
HEDDKYRLDL
262
LAQAGVDVVV
272

LDSSQGNSIF
282
QINMIKYIKD
292
KYPNLQVIGG
302
NVVTAAQAKN
312
LIDAGVDALR
322

VGMGSGSICI
332
TQEVLACGRP
342
QATAVYKVSE
352
YARRFGVPVI
362
ADGGIQNVGH
372

IAKALALGAS
382
TVMMGSLLAA
392
TTEAPGEYFF
402
SDGIRLKKYR
412
GMGSLDAMIK
438

VAQGVSGAVQ
448
DKGSIHKFVP
458
YLIAGIQHSC
468
QDIGAKSLTQ
478
VRAMMYSGEL
488

KFEKRTSSAQ
498
VEGGVHSLHS
508
YEKRLF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IMP or .IMP2 or .IMP3 or :3IMP;style chemicals stick;color identity;select .A:68 or .A:70 or .A:303 or .A:322 or .A:327 or .A:328 or .A:329 or .A:330 or .A:331 or .A:333 or .A:364 or .A:365 or .A:366 or .A:367 or .A:385 or .A:386 or .A:387 or .A:388 or .A:389 or .A:411 or .A:413 or .A:414 or .A:415 or .A:416 or .A:441 or .A:442; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.077
MET70
3.645
ASN303
3.795
ARG322
3.145
SER327
4.502
GLY328
3.836
SER329
2.511
ILE330
3.375
CYS331
3.497
THR333
3.799
ASP364
2.479
GLY365
3.257
GLY366
3.269
Residue
Distance (Å)
ILE367
4.147
MET385
3.476
MET386
3.945
GLY387
2.795
SER388
2.859
LEU389
4.757
TYR411
3.467
GLY413
3.255
MET414
2.724
GLY415
2.449
SER416
4.068
GLN441
2.766
GLY442
3.984
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Ribavirin monophosphate Ligand Info
Structure Description Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with Ribavirin Monophosphate and C2-Mycophenolic Adenine Dinucleotide PDB:1NF7
Method X-ray diffraction Resolution 2.65 Å Mutation No [2]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

YEQGFITDPV
119
VLSPKGIISS
160
RDIDFLEHDC
173
FLEEIMTKRE
183
DLVVAPAGIT
193

LKEANEILQR
203
SKKGKLPIVN
213
EDDELVAIIA
223
RTLKKNRDYP
234
LASKDAKKQL
244

LCGAAIGTHE
254
DDKYRLDLLA
264
QAGVDVVVLD
274
SSQGNSIFQI
284
NMIKYIKDKY
294

PNLQVIGGNV
304
VTAAQAKNLI
314
DAGVDALRVG
324
MGSGSICITQ
334
EVLACGRPQA
344

TAVYKVSEYA
354
RRFGVPVIAD
364
GGIQNVGHIA
374
KALALGASTV
384
MMGSLLAATT
394

EAPGEYFFSD
404
GIRLKKYRGM
414
GSLDAMIKVA
440
QGVSGAVQDK
450
GSIHKFVPYL
460

IAGIQHSCQD
470
IGAKSLTQVR
480
AMMYSGELKF
490
EKRTSSAQVE
500
GGVHSLHSYE
510

KRLF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RVP or .RVP2 or .RVP3 or :3RVP;style chemicals stick;color identity;select .A:68 or .A:69 or .A:70 or .A:303 or .A:322 or .A:327 or .A:328 or .A:329 or .A:330 or .A:331 or .A:332 or .A:333 or .A:364 or .A:365 or .A:366 or .A:367 or .A:385 or .A:386 or .A:387 or .A:388 or .A:411 or .A:413 or .A:414 or .A:415 or .A:416 or .A:441 or .A:442 or .A:443; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
2.626
PRO69
4.541
MET70
3.441
ASN303
3.620
ARG322
3.647
SER327
3.709
GLY328
3.007
SER329
2.973
ILE330
3.329
CYS331
3.279
ILE332
4.270
THR333
4.287
ASP364
2.430
GLY365
3.493
Residue
Distance (Å)
GLY366
3.332
ILE367
4.263
MET385
3.853
MET386
3.921
GLY387
3.316
SER388
3.111
TYR411
2.848
GLY413
3.142
MET414
3.088
GLY415
2.588
SER416
3.701
GLN441
3.046
GLY442
3.335
VAL443
4.798
References  Top
REF 1 Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation. Elife. 2020 Jan 30;9:e53243.
REF 2 Crystal Structure of Human Inosine Monophosphate Dehydrogenase type II complexed with the MPA/NAD analog C2-MAD
REF 3 Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3531-6.
REF 4 The Conformation of NAD Bound to Human Inosine Monophosphate Dehydrogenase Type II
REF 5 A Nucleotide-Dependent Conformational Switch Controls the Polymerization of Human IMP Dehydrogenases to Modulate their Catalytic Activity. J Mol Biol. 2019 Mar 1;431(5):956-969.

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