Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T78543 Target Info
Target Name Protein kinase G1 (PRKG1)
Synonyms cGMP-dependent protein kinase I; cGMP-dependent protein kinase 1; cGKI; cGK1; cGK 1; PRKGR1B; PRKGR1A; PRKG1B
Target Type Literature-reported Target
Gene Name PRKG1
Biochemical Class Kinase
UniProt ID
KGP1_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: AMP-PNP Ligand Info
Structure Description Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain in AMP-PNP bound state PDB:6BG2
Method X-ray diffraction Resolution 1.83 Å Mutation No [1]
PDB Sequence
EDAEAKAKYE
346
AEAAFFANLK
356
LSDFNIIDTL
366
GVGGFGRVEL
376
VQLKSEESKT
386

FAMKILKKRH
396
IVDTRQQEHI
406
RSEKQIMQGA
416
HSDFIVRLYR
426
TFKDSKYLYM
436

LMEACLGGEL
446
WTILRDRGSF
456
EDSTTRFYTA
466
CVVEAFAYLH
476
SKGIIYRDLK
486

PENLILDHRG
496
YAKLVDFGFA
506
KKIGFGKKTW
516
FCGTPEYVAP
527
EIILNKGHDI
537

SADYWSLGIL
547
MYELLTGSPP
557
FSGPDPMKTY
567
NIILRGIDMI
577
EFPKKIAKNA
587

ANLIKKLCRD
597
NPSERLGNLK
607
NGVKDIQKHK
617
WFEGFNWEGL
627
RKGTLTPPII
637

PSVASPTDTS
647
NFDSFPEDND
657
EPPPDDNSGW
667
DIDF
Residue
Distance (Å)
LEU366
3.734
GLY367
3.535
VAL368
4.424
GLY369
3.459
GLY370
3.049
PHE371
2.894
GLY372
3.075
VAL374
3.354
ALA388
3.394
LYS390
2.811
GLU409
4.715
VAL422
3.724
MET438
3.673
Residue
Distance (Å)
GLU439
2.826
ALA440
3.975
CYS441
3.252
GLU445
2.526
ASP484
3.933
LYS486
2.803
GLU488
2.767
ASN489
3.338
ILE491
3.378
VAL501
3.935
ASP502
3.011
PHE649
3.538
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Ligand Name: Phosphonothreonine Ligand Info
Structure Description Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain in AMP-PNP bound state PDB:6BG2
Method X-ray diffraction Resolution 1.83 Å Mutation No [1]
PDB Sequence
EDAEAKAKYE
346
AEAAFFANLK
356
LSDFNIIDTL
366
GVGGFGRVEL
376
VQLKSEESKT
386

FAMKILKKRH
396
IVDTRQQEHI
406
RSEKQIMQGA
416
HSDFIVRLYR
426
TFKDSKYLYM
436

LMEACLGGEL
446
WTILRDRGSF
456
EDSTTRFYTA
466
CVVEAFAYLH
476
SKGIIYRDLK
486

PENLILDHRG
496
YAKLVDFGFA
506
KKIGFGKKTW
516
FCGTPEYVAP
527
EIILNKGHDI
537

SADYWSLGIL
547
MYELLTGSPP
557
FSGPDPMKTY
567
NIILRGIDMI
577
EFPKKIAKNA
587

ANLIKKLCRD
597
NPSERLGNLK
607
NGVKDIQKHK
617
WFEGFNWEGL
627
RKGTLTPPII
637

PSVASPTDTS
647
NFDSFPEDND
657
EPPPDDNSGW
667
DIDF
Residue
Distance (Å)
HIS405
2.719
ARG483
2.777
LYS507
2.678
THR515
2.440
TRP516
1.331
Residue
Distance (Å)
PHE518
1.330
CYS519
3.085
ILE529
4.270
HIS535
3.241
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: [3H]cAMP Ligand Info
Structure Description Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: Insights for PKG agonist design PDB:4QX5
Method X-ray diffraction Resolution 1.32 Å Mutation No [2]
PDB Sequence
IKHTEYMEFL
231
KSVPTFQSLP
241
EEILSKLADV
251
LEETHYENGE
261
YIIRQGARGD
271

TFFIISKGTV
281
NVTREDEDPV
294
FLRTLGKGDW
304
FGEKALQGED
314
VRTANVIAAE
324

AVTCLVIDRD
334
SFKHLIGGLD
344
DVSNKAY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CMP or .CMP2 or .CMP3 or :3CMP;style chemicals stick;color identity;select .A:264 or .A:283 or .A:285 or .A:296 or .A:297 or .A:299 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:310 or .A:315 or .A:316 or .A:317 or .A:318 or .A:320 or .A:351; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE264
3.906
VAL283
3.604
ARG285
4.088
LEU296
3.326
ARG297
3.084
LEU299
4.829
TRP304
4.600
PHE305
3.237
GLY306
2.997
GLU307
2.947
Residue
Distance (Å)
LYS308
3.182
ALA309
2.887
LEU310
4.961
VAL315
4.144
ARG316
2.908
THR317
2.875
ALA318
3.578
VAL320
3.849
TYR351
3.217
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Cyclic Guanosine Monophosphate Ligand Info
Structure Description Structures of PKGI Reveal a cGMP-Selective Activation Mechanism PDB:4KU7
Method X-ray diffraction Resolution 1.65 Å Mutation No [3]
PDB Sequence
KHTEYMEFLK
232
SVPTFQSLPE
242
EILSKLADVL
252
EETHYENGEY
262
IIRQGARGDT
272

FFIISKGTVN
282
VTREDPVFLR
297
TLGKGDWFGE
307
KALQGEDVRT
317
ANVIAAEAVT
327

CLVIDRDSFK
337
HLIGGLDDVS
347
NKAY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PCG or .PCG2 or .PCG3 or :3PCG;style chemicals stick;color identity;select .A:264 or .A:283 or .A:285 or .A:296 or .A:297 or .A:299 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:315 or .A:316 or .A:317 or .A:318 or .A:320 or .A:351; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE264
3.679
VAL283
3.706
ARG285
4.258
LEU296
3.432
ARG297
2.717
LEU299
4.256
TRP304
4.656
PHE305
3.201
GLY306
2.818
Residue
Distance (Å)
GLU307
2.515
LYS308
3.343
ALA309
2.895
VAL315
4.268
ARG316
2.946
THR317
2.598
ALA318
3.444
VAL320
3.651
TYR351
3.137
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: N-((3R,4R)-4-(4-(2-Fluoro-3-methoxy-6-propoxybenzoyl)benzamido)pyrrolidin-3-yl)-1H-indazole-5-carboxamide Ligand Info
Structure Description Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain bound with N46 PDB:6C0T
Method X-ray diffraction Resolution 1.98 Å Mutation No [4]
PDB Sequence
EDAEAKAKYE
346
AEAAFFANLK
356
LSDFNIIDTL
366
GVGGFGRVEL
376
VQLKSEESKT
386

FAMKILKKRH
396
IVDTRQQEHI
406
RSEKQIMQGA
416
HSDFIVRLYR
426
TFKDSKYLYM
436

LMEACLGGEL
446
WTILRDRGSF
456
EDSTTRFYTA
466
CVVEAFAYLH
476
SKGIIYRDLK
486

PENLILDHRG
496
YAKLVDFGFA
506
KKIGFGKKTW
516
FCGTPEYVAP
527
EIILNKGHDI
537

SADYWSLGIL
547
MYELLTGSPP
557
FSGPDPMKTY
567
NIILRGIDMI
577
EFPKKIAKNA
587

ANLIKKLCRD
597
NPSERLGNLK
607
NGVKDIQKHK
617
WFEGFNWEGL
627
RKGTLTPPII
637

PSVASPTDTS
647
NFDSFPEDND
657
EPPPDDNSGW
667
DIDF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .EE4 or .EE42 or .EE43 or :3EE4;style chemicals stick;color identity;select .A:366 or .A:367 or .A:368 or .A:369 or .A:370 or .A:371 or .A:372 or .A:373 or .A:374 or .A:388 or .A:390 or .A:392 or .A:400 or .A:402 or .A:405 or .A:406 or .A:409 or .A:422 or .A:438 or .A:439 or .A:440 or .A:441 or .A:445 or .A:488 or .A:489 or .A:491 or .A:501 or .A:502 or .A:504 or .A:505 or .A:649; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU366
4.000
GLY367
3.582
VAL368
3.541
GLY369
3.438
GLY370
3.348
PHE371
2.706
GLY372
3.667
ARG373
4.183
VAL374
3.359
ALA388
3.304
LYS390
4.297
LEU392
3.966
THR400
4.956
GLN402
3.314
HIS405
3.624
ILE406
3.243
Residue
Distance (Å)
GLU409
4.691
VAL422
3.822
MET438
3.808
GLU439
2.630
ALA440
3.548
CYS441
2.786
GLU445
2.861
GLU488
3.300
ASN489
3.826
ILE491
4.022
VAL501
3.652
ASP502
3.234
GLY504
3.588
PHE505
4.045
PHE649
4.285
Ligand Name: PKG1|A activator 3 Ligand Info
Structure Description Co-structure of PKG1 regulatory domain with compound 33 PDB:7SSB
Method X-ray diffraction Resolution 1.40 Å Mutation Yes [5]
PDB Sequence
STGLIKHTEY
227
MEFLKSVPTF
237
QSLPEEILSK
247
LADVLEETHY
257
ENGEYIIRQG
267

ARGDTFFIIS
277
KGTVNVTRED
287
SDPVFLRTLG
300
KGDWFGEKAL
310
QGEDVRTANV
320

IAAEAVTCLV
330
IDRDSFKHLI
340
GGL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .B4I or .B4I2 or .B4I3 or :3B4I;style chemicals stick;color identity;select .A:236 or .A:237 or .A:240 or .A:248 or .A:252 or .A:273 or .A:275 or .A:304 or .A:307 or .A:310 or .A:311 or .A:331 or .A:336 or .A:340; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
THR236
3.565
PHE237
3.688
LEU240
3.965
LEU248
3.501
LEU252
4.771
PHE273
3.572
ILE275
4.698
Residue
Distance (Å)
TRP304
3.601
GLU307
3.851
LEU310
3.930
GLN311
2.831
ILE331
3.610
PHE336
3.819
ILE340
4.368
Ligand Name: Deuterium Oxide Ligand Info
Structure Description Joint X-ray/neutron structure of PKGIbeta in complex with cGMP PDB:4QXK
Method Neutron diffraction Resolution 2.20 Å Mutation No [2]
PDB Sequence
KHTEYMEFLK
232
SVPTFQSLPE
242
EILSKLADVL
252
EETHYENGEY
262
IIRQGARGDT
272

FFIISKGTVN
282
VTREDSPDPV
294
FLRTLGKGDW
304
FGEKALQGED
314
VRTANVIAAE
324

AVTCLVIDRD
334
SFKHLIGGLD
344
DVSNKAY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .DOD or .DOD2 or .DOD3 or :3DOD;style chemicals stick;color identity;select .A:223 or .A:224 or .A:225 or .A:226 or .A:227 or .A:228 or .A:230 or .A:232 or .A:233 or .A:234 or .A:235 or .A:236 or .A:237 or .A:238 or .A:239 or .A:240 or .A:241 or .A:242 or .A:243 or .A:244 or .A:245 or .A:246 or .A:247 or .A:248 or .A:249 or .A:250 or .A:251 or .A:252 or .A:253 or .A:254 or .A:255 or .A:256 or .A:257 or .A:258 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263 or .A:264 or .A:265 or .A:266 or .A:267 or .A:268 or .A:269 or .A:270 or .A:271 or .A:272 or .A:274 or .A:276 or .A:277 or .A:278 or .A:279 or .A:280 or .A:282 or .A:284 or .A:285 or .A:286 or .A:287 or .A:288 or .A:289 or .A:292 or .A:293 or .A:294 or .A:295 or .A:296 or .A:297 or .A:298 or .A:299 or .A:300 or .A:301 or .A:302 or .A:303 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:310 or .A:311 or .A:312 or .A:313 or .A:314 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:321 or .A:323 or .A:324 or .A:325 or .A:326 or .A:327 or .A:330 or .A:331 or .A:332 or .A:333 or .A:334 or .A:335 or .A:336 or .A:337 or .A:338 or .A:339 or .A:340 or .A:341 or .A:342 or .A:343 or .A:344 or .A:345 or .A:346 or .A:347 or .A:348 or .A:349 or .A:350 or .A:351; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS223
1.943
HIS224
2.207
THR225
2.077
GLU226
2.456
TYR227
2.699
MET228
3.390
PHE230
3.599
LYS232
3.126
SER233
3.300
VAL234
3.566
PRO235
2.703
THR236
1.647
PHE237
2.955
GLN238
1.980
SER239
2.066
LEU240
2.417
PRO241
2.880
GLU242
1.785
GLU243
1.919
ILE244
2.088
LEU245
3.318
SER246
1.861
LYS247
2.320
LEU248
4.588
ALA249
2.086
ASP250
1.884
VAL251
2.562
LEU252
1.970
GLU253
2.412
GLU254
1.525
THR255
2.056
HIS256
2.128
TYR257
1.890
GLU258
1.644
ASN259
2.916
GLY260
4.647
GLU261
2.506
TYR262
1.999
ILE263
1.926
ILE264
2.516
ARG265
1.766
GLN266
2.078
GLY267
2.226
ALA268
2.812
ARG269
2.114
GLY270
3.325
ASP271
2.227
THR272
3.932
PHE274
3.109
ILE276
4.739
SER277
3.533
LYS278
1.778
GLY279
2.040
THR280
2.762
ASN282
3.022
THR284
3.629
ARG285
1.936
GLU286
2.359
ASP287
2.411
Residue
Distance (Å)
SER288
1.942
PRO289
2.625
ASP292
4.049
PRO293
2.565
VAL294
3.221
PHE295
3.248
LEU296
2.778
ARG297
2.400
THR298
2.375
LEU299
2.739
GLY300
2.900
LYS301
1.970
GLY302
2.301
ASP303
2.218
TRP304
1.913
PHE305
2.514
GLY306
4.535
GLU307
3.696
LYS308
2.741
ALA309
2.626
LEU310
2.009
GLN311
2.177
GLY312
1.903
GLU313
2.127
ASP314
2.111
VAL315
1.743
ARG316
2.981
THR317
2.327
ALA318
4.626
ASN319
1.937
ILE321
4.092
ALA323
3.439
GLU324
2.096
ALA325
1.631
VAL326
3.482
THR327
2.127
VAL330
2.199
ILE331
2.293
ASP332
1.728
ARG333
1.819
ASP334
2.160
SER335
3.300
PHE336
2.615
LYS337
2.464
HIS338
1.772
LEU339
2.144
ILE340
3.259
GLY341
1.881
GLY342
1.799
LEU343
3.091
ASP344
3.216
ASP345
1.573
VAL346
2.940
SER347
2.273
ASN348
3.059
LYS349
1.859
ALA350
1.601
TYR351
2.083
Ligand Name: (Rp)-cGMPS Ligand Info
Structure Description PKG I's Carboxyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with RP-cGMP PDB:5L0N
Method X-ray diffraction Resolution 1.28 Å Mutation No [6]
PDB Sequence
GLIKHTEYME
229
FLKSVPTFQS
239
LPEEILSKLA
249
DVLEETHYEN
259
GEYIIRQGAR
269

GDTFFIISKG
279
TVNVTREDSP
289
SEDPVFLRTL
299
GKGDWFGEKA
309
LQGEDVRTAN
319

VIAAEAVTCL
329
VIDRDSFKHL
339
IGGLDDV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6ZA or .6ZA2 or .6ZA3 or :36ZA;style chemicals stick;color identity;select .A:264 or .A:283 or .A:285 or .A:296 or .A:297 or .A:299 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:313 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE264
2.503
VAL283
2.803
ARG285
3.159
LEU296
2.524
ARG297
2.033
LEU299
2.658
TRP304
4.435
PHE305
2.540
GLY306
2.004
GLU307
3.649
Residue
Distance (Å)
LYS308
2.087
ALA309
3.558
GLU313
4.302
VAL315
3.117
ARG316
2.443
THR317
1.769
ALA318
2.541
ASN319
4.637
VAL320
2.572
Ligand Name: 8-bromo-cGMP Ligand Info
Structure Description PKG I's Carboyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with 8-Br-cGMP PDB:5JAX
Method X-ray diffraction Resolution 1.49 Å Mutation No [7]
PDB Sequence
IKHTEYMEFL
231
KSVPTFQSLP
241
EEILSKLADV
251
LEETHYENGE
261
YIIRQGARGD
271

TFFIISKGTV
281
NVTREDSPSE
291
DPVFLRTLGK
301
GDWFGEKALQ
311
GEDVRTANVI
321

AAEAVTCLVI
331
DRDSFKHLIG
341
GLDDVSNKAY
351
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6J7 or .6J72 or .6J73 or :36J7;style chemicals stick;color identity;select .A:264 or .A:283 or .A:285 or .A:296 or .A:297 or .A:299 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:310 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320 or .A:351; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE264
2.785
VAL283
2.744
ARG285
3.095
LEU296
2.531
ARG297
2.103
LEU299
2.868
TRP304
4.764
PHE305
2.398
GLY306
1.862
GLU307
2.123
Residue
Distance (Å)
LYS308
2.520
ALA309
2.167
LEU310
4.671
VAL315
4.172
ARG316
2.042
THR317
1.840
ALA318
2.412
ASN319
4.548
VAL320
2.450
TYR351
2.546
Ligand Name: 8-Pcpt-cgmp Ligand Info
Structure Description PKG I's Carboyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with 8-pCPT-cGMP PDB:5J48
Method X-ray diffraction Resolution 1.49 Å Mutation No [7]
PDB Sequence
GSTGLIKHTE
226
YMEFLKSVPT
236
FQSLPEEILS
246
KLADVLEETH
256
YENGEYIIRQ
266

GARGDTFFII
276
SKGTVNVTRE
286
DDPVFLRTLG
300
KGDWFGEKAL
310
QGEDVRTANV
320

IAAEAVTCLV
330
IDRDSFKHLI
340
GGLDDVSNKA
350
Y
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6FW or .6FW2 or .6FW3 or :36FW;style chemicals stick;color identity;select .A:264 or .A:283 or .A:285 or .A:296 or .A:297 or .A:299 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:310 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320 or .A:349 or .A:351; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE264
2.604
VAL283
2.860
ARG285
2.544
LEU296
2.618
ARG297
2.114
LEU299
2.616
TRP304
2.599
PHE305
2.564
GLY306
2.066
GLU307
2.626
LYS308
2.227
Residue
Distance (Å)
ALA309
2.231
LEU310
4.803
VAL315
3.427
ARG316
2.090
THR317
1.850
ALA318
2.444
ASN319
4.416
VAL320
2.502
LYS349
4.012
TYR351
2.493
Ligand Name: 1,N-(2-Phenyl-1,2-ethenediyl)guanosine 3',5'-phosphoric acid Ligand Info
Structure Description PKG I's Carboxyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with PET-cGMP PDB:5JD7
Method X-ray diffraction Resolution 1.75 Å Mutation No [7]
PDB Sequence
IKHTEYMEFL
231
KSVPTFQSLP
241
EEILSKLADV
251
LEETHYENGE
261
YIIRQGARGD
271

TFFIISKGTV
281
NVTREDEDPV
294
FLRTLGKGDW
304
FGEKALQGED
314
VRTANVIAAE
324

AVTCLVIDRD
334
SFKHLIGGLD
344
DVSNKAY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6JR or .6JR2 or .6JR3 or :36JR;style chemicals stick;color identity;select .A:264 or .A:283 or .A:285 or .A:296 or .A:297 or .A:299 or .A:304 or .A:305 or .A:306 or .A:307 or .A:308 or .A:309 or .A:310 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320 or .A:351; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE264
2.774
VAL283
2.409
ARG285
3.191
LEU296
2.500
ARG297
2.102
LEU299
2.471
TRP304
4.219
PHE305
2.327
GLY306
1.989
GLU307
1.858
Residue
Distance (Å)
LYS308
2.211
ALA309
2.193
LEU310
4.622
VAL315
4.152
ARG316
1.977
THR317
1.446
ALA318
2.362
ASN319
4.352
VAL320
2.509
TYR351
2.484
References  Top
REF 1 Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain
REF 2 Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: insights for cGMP-dependent protein kinase agonist design. Biochemistry. 2014 Nov 4;53(43):6725-7.
REF 3 Structural basis for cyclic-nucleotide selectivity and cGMP-selective activation of PKG I. Structure. 2014 Jan 7;22(1):116-24.
REF 4 Structural basis for selective inhibition of human PKG IAlpha by the balanol-like compound N46. J Biol Chem. 2018 Jul 13;293(28):10985-10992.
REF 5 Optimization and Mechanistic Investigations of Novel Allosteric Activators of PKG1Alpha. J Med Chem. 2022 Aug 11;65(15):10318-10340.
REF 6 Structure of PKG I CNB-B bound to RP-cGMP
REF 7 Structural Basis of Analog Specificity in PKG I and II. ACS Chem Biol. 2017 Sep 15;12(9):2388-2398.

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