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 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
Ligand General Information  Top
Ligand Name Inosinic Acid Ligand Info
Canonical SMILES C1=NC2=C(C(=O)N1)N=CN2C3C(C(C(O3)COP(=O)(O)O)O)O
InChI 1S/C10H13N4O8P/c15-6-4(1-21-23(18,19)20)22-10(7(6)16)14-3-13-5-8(14)11-2-12-9(5)17/h2-4,6-7,10,15-16H,1H2,(H,11,12,17)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey GRSZFWQUAKGDAV-KQYNXXCUSA-N
PubChem Compound ID 135398640
Drug Binding Sites of Target  Top
PDB ID: 6U8S      Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Filament assembly interface reconstruction.
Method Electron microscopy Resolution 3.14 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
Residue
Distance (Å)
SER68
3.076
MET70
3.457
ASN303
4.246
ARG322
3.022
GLY324
4.232
SER327
4.540
GLY328
3.320
SER329
2.505
ILE330
4.328
CYS331
1.628
ILE332
4.899
THR333
4.795
ASP364
3.308
GLY365
3.399
Residue
Distance (Å)
GLY366
3.760
ILE367
4.193
MET385
3.603
MET386
4.321
GLY387
3.134
SER388
2.850
LEU389
4.409
TYR411
2.415
GLY413
3.057
MET414
2.757
GLY415
2.342
SER416
3.913
GLN441
2.936
GLY442
3.847
PDB ID: 6UDP      Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Filament assembly interface reconstruction.
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
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
PDB ID: 6U8E      Human IMPDH2 treated with ATP, IMP, and NAD+. Filament assembly interface reconstruction.
Method Electron microscopy Resolution 3.03 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
PLASKDAKKQ
243
LLCGAAIGTH
253
EDDKYRLDLL
263
AQAGVDVVVL
273

DSSQGNSIFQ
283
INMIKYIKDK
293
YPNLQVIGGN
303
VVTAAQAKNL
313
IDAGVDALRV
323

GMGSGSICIT
333
QEVLACGRPQ
343
ATAVYKVSEY
353
ARRFGVPVIA
363
DGGIQNVGHI
373

AKALALGAST
383
VMMGSLLAAT
393
TEAPGEYFFS
403
DGIRLKKYRG
413
MGSLDAMIKV
439

AQGVSGAVQD
449
KGSIHKFVPY
459
LIAGIQHSCQ
469
DIGAKSLTQV
479
RAMMYSGELK
489

FEKRTSSAQV
499
EGGVHSLHSY
509
EKRLF
Residue
Distance (Å)
SER68
3.478
PRO69
4.928
MET70
3.750
ASN303
3.966
ARG322
3.014
GLY324
4.764
SER327
4.158
GLY328
3.302
SER329
2.524
ILE330
3.453
CYS331
1.360
ILE332
4.396
THR333
4.350
ASP364
2.352
GLY365
3.323
Residue
Distance (Å)
GLY366
3.352
ILE367
4.599
MET385
3.546
MET386
3.709
GLY387
2.664
SER388
2.610
LEU389
4.959
TYR411
2.840
GLY413
3.471
MET414
3.031
GLY415
2.483
SER416
3.862
GLN441
2.408
GLY442
3.762
PDB ID: 6UDO      Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Fully compressed filament segment reconstruction.
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
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:324 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 #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.057
MET70
3.475
ASN303
3.913
ARG322
3.112
GLY324
4.193
SER327
4.366
GLY328
3.317
SER329
2.525
ILE330
3.405
CYS331
1.627
THR333
3.525
ASP364
2.500
GLY365
3.442
GLY366
3.312
Residue
Distance (Å)
ILE367
4.595
MET385
3.733
MET386
4.146
GLY387
3.201
SER388
2.754
LEU389
4.704
TYR411
3.255
GLY413
3.498
MET414
2.865
GLY415
2.415
SER416
4.315
GLN441
2.835
GLY442
4.124
PDB ID: 6U9O      Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Fully compressed filament segment reconstruction.
Method Electron microscopy Resolution 3.36 Å Mutation No [1]
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
LRVGMGSGSI
330
CITQEVLACG
340
RPQATAVYKV
350
SEYARRFGVP
360

VIADGGIQNV
370
GHIAKALALG
380
ASTVMMGSLL
390
AATTEAPGEY
400
FFSDGIRLKK
410

YRGMGSLDAM
420
IKVAQGVSGA
446
VQDKGSIHKF
456
VPYLIAGIQH
466
SCQDIGAKSL
476

TQVRAMMYSG
486
ELKFEKRTSS
496
AQVEGGVHSL
506
HSYEKRLF
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: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: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
2.764
PRO69
4.661
MET70
3.457
ASN303
4.638
ARG322
3.210
SER327
4.357
GLY328
3.263
SER329
2.514
ILE330
3.486
CYS331
1.628
ILE332
4.834
THR333
4.789
ASP364
2.604
GLY365
3.328
Residue
Distance (Å)
GLY366
3.325
ILE367
4.180
MET385
4.034
MET386
4.164
GLY387
2.980
SER388
2.772
LEU389
4.763
TYR411
2.431
GLY413
3.293
MET414
2.969
GLY415
2.521
SER416
3.709
GLN441
2.351
GLY442
3.483
PDB ID: 6UA4      Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Bent (3/4 compressed, 1/4 extended) segment reconstruction.
Method Electron microscopy Resolution 3.65 Å Mutation No [1]
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
LRVGMGSGSI
330
CITQEVLACG
340
RPQATAVYKV
350
SEYARRFGVP
360

VIADGGIQNV
370
GHIAKALALG
380
ASTVMMGSLL
390
AATTEAPGEY
400
FFSDGIRLKK
410

YRGMGSLDAM
420
IKVAQGVSGA
446
VQDKGSIHKF
456
VPYLIAGIQH
466
SCQDIGAKSL
476

TQVRAMMYSG
486
ELKFEKRTSS
496
AQVEGGVHSL
506
HSYEKRLF
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:324 or .A:327 or .A:328 or .A:329 or .A:330 or .A:331 or .A:332 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 #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
2.881
MET70
3.440
ASN303
4.310
ARG322
2.940
GLY324
4.439
SER327
4.242
GLY328
3.528
SER329
2.719
ILE330
3.521
CYS331
3.495
ILE332
4.837
ASP364
2.362
GLY365
3.308
GLY366
3.371
Residue
Distance (Å)
ILE367
4.314
MET385
3.853
MET386
3.904
GLY387
2.794
SER388
2.579
LEU389
4.197
TYR411
2.508
GLY413
3.083
MET414
2.806
GLY415
2.412
SER416
3.858
GLN441
2.779
GLY442
3.714
PDB ID: 6UA5      Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free interfacial octamer reconstruction.
Method Electron microscopy Resolution 3.79 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:324 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
3.243
MET70
3.472
ASN303
4.743
ARG322
2.865
GLY324
4.799
SER327
4.342
GLY328
3.236
SER329
2.467
ILE330
4.413
CYS331
1.626
THR333
4.753
ASP364
2.724
GLY365
3.328
GLY366
3.710
Residue
Distance (Å)
ILE367
3.845
MET385
3.848
MET386
4.451
GLY387
3.214
SER388
2.596
LEU389
4.802
TYR411
3.236
GLY413
3.189
MET414
2.907
GLY415
2.483
SER416
3.900
GLN441
3.693
GLY442
3.808
PDB ID: 6UAJ      Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free canonical octamer reconstruction.
Method Electron microscopy Resolution 3.84 Å Mutation No [1]
PDB Sequence
TSYVPDDGLT
19
AQQLFNCGDG
29
LTYNDFLILP
39
GYIDFTADQV
49
DLTSALTKKI
59

TLKTPLVSSP
69
MDTVTEAGMA
79
IAMALTGGIG
89
FIHHNCTPEF
99
QANEVRKVKK
109

YEQGFITDPV
119
VLSPKDRVRD
129
VFEAKARHGF
139
CGIPITDTGR
149
MGSRLVGIIS
159

SRDIDFLKEE
169
EHDCFLEEIM
179
TKREDLVVAP
189
AGITLKEANE
199
ILQRSKKGKL
209

PIVNEDDELV
219
AIIARTDLKK
229
NRDYPLASKD
239
AKKQLLCGAA
249
IGTHEDDKYR
259

LDLLAQAGVD
269
VVVLDSSQGN
279
SIFQINMIKY
289
IKDKYPNLQV
299
IGGNVVTAAQ
309

AKNLIDAGVD
319
ALRVGMGSGS
329
ICITQEVLAC
339
GRPQATAVYK
349
VSEYARRFGV
359

PVIADGGIQN
369
VGHIAKALAL
379
GASTVMMGSL
389
LAATTEAPGE
399
YFFSDGIRLK
409

KYRGMGSLDA
419
MIKVAQGVSG
445
AVQDKGSIHK
455
FVPYLIAGIQ
465
HSCQDIGAKS
475

LTQVRAMMYS
485
GELKFEKRTS
495
SAQVEGGVHS
505
LHSYEKRLF
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:69 or .A:70 or .A:322 or .A:324 or .A:328 or .A:329 or .A:330 or .A:331 or .A:332 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 #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.291
PRO69
4.935
MET70
3.488
ARG322
3.351
GLY324
4.704
GLY328
4.029
SER329
3.843
ILE330
3.594
CYS331
3.242
ILE332
4.991
ASP364
2.279
GLY365
2.897
GLY366
3.730
Residue
Distance (Å)
ILE367
3.649
MET385
3.856
MET386
3.781
GLY387
3.018
SER388
2.790
LEU389
4.432
TYR411
3.545
GLY413
3.102
MET414
2.625
GLY415
2.368
SER416
4.788
GLN441
3.750
GLY442
3.701
PDB ID: 6U8R      Human IMPDH2 treated with ATP, IMP, and NAD+. Bent (1/4 compressed, 3/4 extended) segment reconstruction.
Method Electron microscopy Resolution 3.91 Å Mutation No [1]
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
LRVGMGSGSI
330
CITQEVLACG
340
RPQATAVYKV
350
SEYARRFGVP
360

VIADGGIQNV
370
GHIAKALALG
380
ASTVMMGSLL
390
AATTEAPGEY
400
FFSDGIRLKK
410

YRGMGSLDAM
420
IKVAQGVSGA
446
VQDKGSIHKF
456
VPYLIAGIQH
466
SCQDIGAKSL
476

TQVRAMMYSG
486
ELKFEKRTSS
496
AQVEGGVHSL
506
HSYEKRLF
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:69 or .A:70 or .A:303 or .A:322 or .A:324 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; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.385
PRO69
4.887
MET70
3.427
ASN303
4.043
ARG322
3.247
GLY324
4.582
SER327
4.564
GLY328
3.151
SER329
2.383
ILE330
4.375
CYS331
3.195
ILE332
4.912
THR333
4.433
ASP364
2.731
Residue
Distance (Å)
GLY365
3.360
GLY366
3.610
ILE367
4.700
MET385
3.814
MET386
4.031
GLY387
2.892
SER388
2.258
TYR411
2.827
GLY413
3.042
MET414
2.776
GLY415
2.366
SER416
3.907
GLN441
2.901
GLY442
3.844
PDB ID: 6UA2      Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Bent (2/4 compressed, 2/4 extended) segment reconstruction.
Method Electron microscopy Resolution 4.20 Å Mutation No [1]
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
LRVGMGSGSI
330
CITQEVLACG
340
RPQATAVYKV
350
SEYARRFGVP
360

VIADGGIQNV
370
GHIAKALALG
380
ASTVMMGSLL
390
AATTEAPGEY
400
FFSDGIRLKK
410

YRGMGSLDAM
420
IKVAQGVSGA
446
VQDKGSIHKF
456
VPYLIAGIQH
466
SCQDIGAKSL
476

TQVRAMMYSG
486
ELKFEKRTSS
496
AQVEGGVHSL
506
HSYEKRLF
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:322 or .A:324 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:389 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
2.627
MET70
4.397
ARG322
3.300
GLY324
4.849
SER327
4.371
GLY328
3.225
SER329
2.399
ILE330
3.550
CYS331
3.507
ILE332
4.894
THR333
4.828
ASP364
2.689
GLY365
3.348
GLY366
2.736
Residue
Distance (Å)
ILE367
4.180
MET385
3.889
MET386
4.302
GLY387
3.062
SER388
2.273
LEU389
4.558
TYR411
2.916
GLY413
3.128
MET414
3.156
GLY415
2.580
SER416
3.997
GLN441
2.997
GLY442
3.370
VAL443
4.909
References  Top
REF 1 Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation. Elife. 2020 Jan 30;9:e53243.

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