Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T10265 | Target Info | |||
| Target Name | Phosphodiesterase 4B (PDE4B) | ||||
| Synonyms | cAMP-specific 3',5'-cyclic phosphodiesterase 4B; Type 4B cAMP phosphodiesterase; Type 4 cyclic adenosine monophosphate phosphodiesterase (type 4 PDE); PDE32; DPDE4 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | PDE4B | ||||
| Biochemical Class | Phosphoric diester hydrolase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | S,S-(2-Hydroxyethyl)Thiocysteine | Ligand Info | |||
| Canonical SMILES | C(CSSCC(C(=O)O)N)O | ||||
| InChI | 1S/C5H11NO3S2/c6-4(5(8)9)3-11-10-2-1-7/h4,7H,1-3,6H2,(H,8,9)/t4-/m0/s1 | ||||
| InChIKey | YPUBRSXDQSFQBA-BYPYZUCNSA-N | ||||
| PubChem Compound ID | 170018 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 1XM6 Catalytic Domain Of Human Phosphodiesterase 4B In Complex With (R)-Mesopram | ||||||
| Method | X-ray diffraction | Resolution | 1.92 Å | Mutation | No | [1] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHDIFM 324 NLTKKQRQTL334 RKMVIDMVLA344 TDMSKHMSLL354 ADLKTMVETK364 KVTSSGVLLL 374 DNYTDRIQVL384 RNMVHCADLS394 NPTKSLELYR404 QWTDRIMEEF414 FQQGDKERER 424 GMEISPMDKH435 TASVEKSQVG445 FIDYIVHPLW455 ETWADLVQPD465 AQDILDTLED 475 NRNWYQSMIP485 CQGLMEKFQF508 ELTLD
|
|||||
|
|
LEU166
3.823
LEU170
3.770
VAL183
4.003
SER187
3.944
ARG190
3.200
PRO191
3.760
LEU192
3.434
THR193
1.316
ILE195
1.342
MET196
3.332
TYR197
3.229
ALA198
2.965
GLN201
4.413
THR215
3.947
THR218
4.011
TYR219
3.460
THR222
3.709
SER282
4.033
LEU314
3.340
LEU315
3.730
GLN316
4.886
|
|||||
| PDB ID: 1XLZ Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Filaminast | ||||||
| Method | X-ray diffraction | Resolution | 2.06 Å | Mutation | Yes | [1] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHDIFM 324 NLTKKQRQTL334 RKMVIDMVLA344 TDMSKHMSLL354 ADLKTMVETK364 KVTSSGVLLL 374 DNYTDRIQVL384 RNMVHCADLS394 NPTKSLELYR404 QWTDRIMEEF414 FQQGDKERER 424 GMEISPMCDK434 HTASVEKSQV444 GFIDYIVHPL454 WETWADLVQP464 DAQDILDTLE 474 DNRNWYQSMI484 P
|
|||||
|
|
LEU166
4.226
LEU170
4.499
VAL183
4.276
SER187
3.902
ARG190
2.967
PRO191
3.392
LEU192
3.306
THR193
1.332
ILE195
1.328
MET196
3.292
TYR197
3.347
ALA198
2.981
|
|||||
| PDB ID: 1XLX Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Cilomilast | ||||||
| Method | X-ray diffraction | Resolution | 2.19 Å | Mutation | Yes | [1] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHCDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTSSGVLL 373 LDNYTDRIQV383 LRNMVHCADL393 SNPTKSLELY403 RQWTDRIMEE413 FFQQGDKERE 423 RGMEISPMCD433 KHTASVEKSQ443 VGFIDYIVHP453 LWETWADLVQ463 PDAQDILDTL 473 EDNRNWYQSM483 IP
|
|||||
|
|
||||||
| PDB ID: 1XOS Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Sildenafil | ||||||
| Method | X-ray diffraction | Resolution | 2.28 Å | Mutation | Yes | [1] |
| PDB Sequence |
NEDHLAKELE
171 DLNKWGLNIF181 NVAGYSHNRP191 LTIMYAIFQE202 RDLLKTFRIS212 SDTFITYMMT 222 LEDHYHSDVA232 YHNSLHAADV242 AQSTHVLLST252 PALDAVFTDL262 EILAAIFAAA 272 IHDVDHPGVS282 NQFLINTNSE292 LALMYNDESV302 LENHHLAVGF312 KLLQEEHDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTGVLLLD 375 NYTDRIQVLR385 NMVHCADLSN395 PTKSLELYRQ405 WTDRIMEEFF415 QQGDKERERG 425 MEISPMDKHT436 ASVEKSQVGF446 IDYIVHPLWE456 TWADLVQPDA466 QDILDTLEDN 476 RNWYQSMIP
|
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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 .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:201 or .A:215 or .A:218 or .A:219 or .A:222 or .A:282 or .A:314 or .A:315 or .A:317 or .A:318 or .A:319 or .A:321 or .A:322 or .A:414 or .A:415 or .A:417 or .A:418 or .A:419 or .A:421 or .A:428 or .A:429 or .A:430 or .A:431 or .A:433 or .A:434 or .A:437; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU166
3.918
LEU170
3.772
VAL183
4.395
SER187
4.211
ARG190
3.206
PRO191
3.813
LEU192
3.547
THR193
1.327
ILE195
1.333
MET196
3.077
TYR197
3.151
ALA198
2.993
GLN201
4.091
THR215
3.895
THR218
3.852
TYR219
3.596
THR222
3.536
SER282
3.918
LEU314
3.489
|
|||||
| PDB ID: 1XMU Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Roflumilast | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
RFGVNTENED 164 HLAKELEDLN174 KWGLNIFNVA184 GYSHNRPLTI195 MYAIFQERDL205 LKTFRISSDT 215 FITYMMTLED225 HYHSDVAYHN235 SLHAADVAQS245 THVLLSTPAL255 DAVFTDLEIL 265 AAIFAAAIHD275 VDHPGVSNQF285 LINTNSELAL295 MYNDESVLEN305 HHLAVGFKLL 315 QEEHCDIFMN325 LTKKQRQTLR335 KMVIDMVLAT345 DMSKHMSLLA355 DLKTMVETKK 365 VTSSGVLLLD375 NYTDRIQVLR385 NMVHCADLSN395 PTKSLELYRQ405 WTDRIMEEFF 415 QQGDKERERG425 MEISPMDKHT436 ASVEKSQVGF446 IDYIVHPLWE456 TWADLVQPDA 466 QDILDTLEDN476 RNWYQSMIP> Chain B EDHLAKELED 172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHDIFM 324 NLTKKQRQTL334 RKMVIDMVLA344 TDMSKHMSLL354 ADLKTMVETK364 KVTSSGVLLL 374 DNYTDRIQVL384 RNMVHCADLS394 NPTKSLELYR404 QWTDRIMEEF414 FQQGDKERER 424 GMEISPMCDK434 HTASVEKSQV444 GFIDYIVHPL454 WETWADLVQP464 DAQDILDTLE 474 DNRNWYQSMI484 P
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:156 or .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:201 or .A:282 or .A:414 or .A:415 or .A:417 or .A:418 or .A:419 or .A:421 or .A:428 or .A:429 or .A:430 or .A:431 or .A:433 or .A:434 or .A:437 or .B:166 or .B:170 or .B:183 or .B:187 or .B:190 or .B:191 or .B:192 or .B:193 or .B:195 or .B:196 or .B:197 or .B:198 or .B:201 or .B:215 or .B:218 or .B:219 or .B:222 or .B:314 or .B:315 or .B:317 or .B:318 or .B:319 or .B:321 or .B:322; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE156[A]
3.551
LEU166[A]
3.843
LEU170[A]
3.848
VAL183[A]
4.092
SER187[A]
4.161
ARG190[A]
3.177
PRO191[A]
3.960
LEU192[A]
3.601
THR193[A]
1.316
ILE195[A]
1.347
MET196[A]
3.284
TYR197[A]
3.131
ALA198[A]
2.998
GLN201[A]
4.299
SER282[A]
3.748
PHE414[A]
3.474
PHE415[A]
3.659
GLN417[A]
4.032
GLY418[A]
3.206
ASP419[A]
4.870
GLU421[A]
4.559
ILE428[A]
4.103
SER429[A]
3.299
PRO430[A]
3.491
MET431[A]
1.325
ASP433[A]
1.352
LYS434[A]
3.678
ALA437[A]
4.971
LEU166[B]
3.676
LEU170[B]
3.867
VAL183[B]
4.858
SER187[B]
4.234
ARG190[B]
3.091
PRO191[B]
3.756
LEU192[B]
3.514
THR193[B]
1.312
ILE195[B]
1.353
MET196[B]
3.301
TYR197[B]
3.123
ALA198[B]
2.898
GLN201[B]
4.648
THR215[B]
3.720
THR218[B]
3.657
TYR219[B]
3.653
THR222[B]
3.254
LEU314[B]
3.107
LEU315[B]
3.959
GLU317[B]
3.113
GLU318[B]
2.869
HIS319[B]
1.335
ASP321[B]
1.342
ILE322[B]
2.734
|
|||||
| PDB ID: 1XM4 Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Piclamilast | ||||||
| Method | X-ray diffraction | Resolution | 2.31 Å | Mutation | Yes | [1] |
| PDB Sequence |
> Chain A
EDHLAKELED 172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHCDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTSSGVLL 373 LDNYTDRIQV383 LRNMVHCADL393 SNPTKSLELY403 RQWTDRIMEE413 FFQQGDKERE 423 RGMEISPMDK434 HTASVEKSQV444 GFIDYIVHPL454 WETWADLVQP464 DAQDILDTLE 474 DNRNWYQSMI484 P> Chain B EDHLAKELED 172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHDIFM 324 NLTKKQRQTL334 RKMVIDMVLA344 TDMSKHMSLL354 ADLKTMVETK364 KVTSSGVLLL 374 DNYTDRIQVL384 RNMVHCADLS394 NPTKSLELYR404 QWTDRIMEEF414 FQQGDKERER 424 GMEISPMCDK434 HTASVEKSQV444 GFIDYIVHPL454 WETWADLVQP464 DAQDILDTLE 474 DNRNWYQSMI484 P
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:199 or .A:224 or .A:282 or .A:414 or .A:415 or .A:417 or .A:418 or .A:419 or .A:421 or .A:428 or .A:429 or .A:430 or .A:431 or .A:433 or .A:434 or .B:166 or .B:170 or .B:183 or .B:187 or .B:190 or .B:191 or .B:192 or .B:193 or .B:195 or .B:196 or .B:197 or .B:198 or .B:201 or .B:215 or .B:218 or .B:219 or .B:222 or .B:224 or .B:313 or .B:314 or .B:315 or .B:316 or .B:317 or .B:318 or .B:319 or .B:321 or .B:322; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU166[A]
3.818
LEU170[A]
3.843
VAL183[A]
4.369
SER187[A]
3.857
ARG190[A]
2.967
PRO191[A]
3.433
LEU192[A]
3.398
THR193[A]
1.342
ILE195[A]
1.337
MET196[A]
3.339
TYR197[A]
3.283
ALA198[A]
2.891
ILE199[A]
4.975
GLU224[A]
4.961
SER282[A]
3.517
PHE414[A]
3.170
PHE415[A]
3.442
GLN417[A]
3.691
GLY418[A]
3.289
ASP419[A]
4.813
GLU421[A]
4.274
ILE428[A]
4.050
SER429[A]
2.710
PRO430[A]
3.200
MET431[A]
1.352
ASP433[A]
1.343
LYS434[A]
3.482
LEU166[B]
3.866
LEU170[B]
3.801
VAL183[B]
4.480
SER187[B]
4.189
ARG190[B]
2.759
PRO191[B]
3.705
LEU192[B]
3.428
THR193[B]
1.336
ILE195[B]
1.323
MET196[B]
3.312
TYR197[B]
3.385
ALA198[B]
3.042
GLN201[B]
4.672
THR215[B]
3.832
THR218[B]
3.716
TYR219[B]
3.397
THR222[B]
3.565
GLU224[B]
4.973
LYS313[B]
4.389
LEU314[B]
2.907
LEU315[B]
3.808
GLN316[B]
4.324
GLU317[B]
2.683
GLU318[B]
3.023
HIS319[B]
1.336
ASP321[B]
1.338
ILE322[B]
3.013
|
|||||
| PDB ID: 1XN0 Catalytic Domain Of Human Phosphodiesterase 4B In Complex With (R,S)-Rolipram | ||||||
| Method | X-ray diffraction | Resolution | 2.31 Å | Mutation | No | [1] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHDIFM 324 NLTKKQRQTL334 RKMVIDMVLA344 TDMSKHMSLL354 ADLKTMVETK364 KVTSSGVLLL 374 DNYTDRIQVL384 RNMVHCADLS394 NPTKSLELYR404 QWTDRIMEEF414 FQQGDKERER 424 GMEISPMDKH435 TASVEKSQVG445 FIDYIVHPLW455 ETWADLVQPD465 AQDILDTLED 475 NRNWYQSMIP485
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:215 or .A:218 or .A:219 or .A:222 or .A:282 or .A:314 or .A:315 or .A:317 or .A:318 or .A:319 or .A:321 or .A:322 or .A:414 or .A:415 or .A:417 or .A:418 or .A:419 or .A:421 or .A:428 or .A:429 or .A:430 or .A:431 or .A:433 or .A:434 or .A:437; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU166
4.022
LEU170
3.877
VAL183
4.515
SER187
3.970
ARG190
3.195
PRO191
3.570
LEU192
3.506
THR193
1.320
ILE195
1.352
MET196
3.355
TYR197
3.168
ALA198
2.951
THR215
4.063
THR218
4.229
TYR219
3.455
THR222
3.555
SER282
3.678
LEU314
3.194
LEU315
3.930
|
|||||
| PDB ID: 1XOT Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Vardenafil | ||||||
| Method | X-ray diffraction | Resolution | 2.34 Å | Mutation | Yes | [1] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHCDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTSSGVLL 373 LDNYTDRIQV383 LRNMVHCADL393 SNPTKSLELY403 RQWTDRIMEE413 FFQQGDKERE 423 RGMEISPMCD433 KHTASVEKSQ443 VGFIDYIVHP453 LWETWADLVQ463 PDAQDILDTL 473 EDNRNWYQSM483 IP
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .B:166 or .B:170 or .B:183 or .B:187 or .B:190 or .B:191 or .B:192 or .B:193 or .B:195 or .B:196 or .B:197 or .B:198 or .B:201; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| PDB ID: 1XMY Catalytic Domain Of Human Phosphodiesterase 4B In Complex With (R)-Rolipram | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | Yes | [1] |
| PDB Sequence |
> Chain A
EDHLAKELED 172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHDIFM 324 NLTKKQRQTL334 RKMVIDMVLA344 TDMSKHMSLL354 ADLKTMVETK364 KVTSSGVLLL 374 DNYTDRIQVL384 RNMVHCADLS394 NPTKSLELYR404 QWTDRIMEEF414 FQQGDKERER 424 GMEISPMCDK434 HTASVEKSQV444 GFIDYIVHPL454 WETWADLVQP464 DAQDILDTLE 474 DNRNWYQSMI484 P> Chain B EDHLAKELED 172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHCDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTSSGVLL 373 LDNYTDRIQV383 LRNMVHCADL393 SNPTKSLELY403 RQWTDRIMEE413 FFQQGDKERE 423 RGMEISPMDK434 HTASVEKSQV444 GFIDYIVHPL454 WETWADLVQP464 DAQDILDTLE 474 DNRNWYQSMI484 P
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:215 or .A:218 or .A:219 or .A:222 or .A:314 or .A:315 or .A:317 or .A:318 or .A:319 or .A:321 or .A:322 or .B:166 or .B:170 or .B:183 or .B:187 or .B:190 or .B:191 or .B:192 or .B:193 or .B:195 or .B:196 or .B:197 or .B:198 or .B:414 or .B:415 or .B:417 or .B:418 or .B:419 or .B:421 or .B:422 or .B:428 or .B:429 or .B:430 or .B:431 or .B:433 or .B:434 or .B:437; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU166[A]
3.880
LEU170[A]
4.242
VAL183[A]
4.958
SER187[A]
3.956
ARG190[A]
2.985
PRO191[A]
3.430
LEU192[A]
3.508
THR193[A]
1.340
ILE195[A]
1.339
MET196[A]
3.300
TYR197[A]
3.216
ALA198[A]
2.940
THR215[A]
4.074
THR218[A]
4.363
TYR219[A]
3.292
THR222[A]
4.547
LEU314[A]
3.014
LEU315[A]
3.633
GLU317[A]
3.546
GLU318[A]
2.917
HIS319[A]
1.356
ASP321[A]
1.331
ILE322[A]
2.990
LEU166[B]
3.948
LEU170[B]
4.550
VAL183[B]
4.618
SER187[B]
3.916
ARG190[B]
2.751
PRO191[B]
3.710
LEU192[B]
3.530
THR193[B]
1.349
ILE195[B]
1.338
MET196[B]
3.378
TYR197[B]
3.203
ALA198[B]
3.000
PHE414[B]
2.857
PHE415[B]
3.445
GLN417[B]
4.609
GLY418[B]
3.461
ASP419[B]
4.839
GLU421[B]
4.989
ARG422[B]
4.876
ILE428[B]
4.018
SER429[B]
2.512
PRO430[B]
3.245
MET431[B]
1.343
ASP433[B]
1.333
LYS434[B]
3.139
ALA437[B]
4.801
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| PDB ID: 1Y2H Catalytic Domain Of Human Phosphodiesterase 4B In Complex With 1-(2-chloro-phenyl)-3,5-dimethyl-1H-pyrazole-4-carboxylic acid ethyl ester | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [2] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHCDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTSSGVLL 373 LDNYTDRIQV383 LRNMVHCADL393 SNPTKSLELY403 RQWTDRIMEE413 FFQQGDKERE 423 RGMEISPMCD433 KHTASVEKSQ443 VGFIDYIVHP453 LWETWADLVQ463 PDAQDILDTL 473 EDNRNWYQSM483 IP
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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 .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:201; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 1Y2J Catalytic Domain Of Human Phosphodiesterase 4B In Complex With 3,5-dimethyl-1-(3-nitro-phenyl)-1H-pyrazole-4-carboxylic acid ethyl ester | ||||||
| Method | X-ray diffraction | Resolution | 2.55 Å | Mutation | Yes | [2] |
| PDB Sequence |
EDHLAKELED
172 LNKWGLNIFN182 VAGYSHNRPL192 TIMYAIFQER203 DLLKTFRISS213 DTFITYMMTL 223 EDHYHSDVAY233 HNSLHAADVA243 QSTHVLLSTP253 ALDAVFTDLE263 ILAAIFAAAI 273 HDVDHPGVSN283 QFLINTNSEL293 ALMYNDESVL303 ENHHLAVGFK313 LLQEEHCDIF 323 MNLTKKQRQT333 LRKMVIDMVL343 ATDMSKHMSL353 LADLKTMVET363 KKVTSSGVLL 373 LDNYTDRIQV383 LRNMVHCADL393 SNPTKSLELY403 RQWTDRIMEE413 FFQQGDKERE 423 RGMEISPMCD433 KHTASVEKSQ443 VGFIDYIVHP453 LWETWADLVQ463 PDAQDILDTL 473 EDNRNWYQSM483 IP
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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 .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:166 or .A:170 or .A:183 or .A:187 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:197 or .A:198 or .A:199 or .A:201; 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 | Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. | ||||
| REF 2 | A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. | ||||
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