eF-site ID 6hwo-C PDB Code 6hwo Chain C click to enlarge Title Crystal structure of human phosphodiesterase 4D2 catalytic domain with inhibitor NPD-1335 Classification HYDROLASE Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D Source (PDE4D_HUMAN) Sequence C:  EQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIF QERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAA DVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPG VSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENC DIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTM VETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPL QLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVE KSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWY QSTI Description Functional site 1) chain C residue 215 type sequence T description binding site for residue EDO A 511 source : AD2 2) chain C residue 217 type sequence S description binding site for residue EDO A 511 source : AD2 3) chain C residue 350 type sequence R description binding site for residue EDO A 511 source : AD2 4) chain C residue 239 type sequence K description binding site for residue EDO A 516 source : AD7 5) chain C residue 156 type sequence D description binding site for residue PEG A 521 source : AE3 6) chain C residue 214 type sequence N description binding site for residue EDO C 501 source : AG2 7) chain C residue 350 type sequence R description binding site for residue EDO C 501 source : AG2 8) chain C residue 352 type sequence M description binding site for residue EDO C 501 source : AG2 9) chain C residue 115 type sequence N description binding site for residue EDO C 502 source : AG3 10) chain C residue 150 type sequence E description binding site for residue EDO C 502 source : AG3 11) chain C residue 151 type sequence D description binding site for residue EDO C 502 source : AG3 12) chain C residue 153 type sequence Y description binding site for residue EDO C 502 source : AG3 13) chain C residue 162 type sequence N description binding site for residue EDO C 502 source : AG3 14) chain C residue 105 type sequence H description binding site for residue EPE C 503 source : AG4 15) chain C residue 107 type sequence F description binding site for residue EPE C 503 source : AG4 16) chain C residue 108 type sequence R description binding site for residue EPE C 503 source : AG4 17) chain C residue 111 type sequence E description binding site for residue EPE C 503 source : AG4 18) chain C residue 327 type sequence Q description binding site for residue EPE C 503 source : AG4 19) chain C residue 328 type sequence L description binding site for residue EPE C 503 source : AG4 20) chain C residue 331 type sequence Q description binding site for residue EPE C 503 source : AG4 21) chain C residue 262 type sequence K description binding site for residue EDO C 504 source : AG5 22) chain C residue 266 type sequence D description binding site for residue EDO C 504 source : AG5 23) chain C residue 269 type sequence L description binding site for residue EDO C 505 source : AG6 24) chain C residue 275 type sequence K description binding site for residue EDO C 505 source : AG6 25) chain C residue 134 type sequence T description binding site for residue EDO C 506 source : AG7 26) chain C residue 135 type sequence F description binding site for residue EDO C 506 source : AG7 27) chain C residue 136 type sequence K description binding site for residue EDO C 506 source : AG7 28) chain C residue 251 type sequence N description binding site for residue EDO C 506 source : AG7 29) chain C residue 256 type sequence Q description binding site for residue EDO C 506 source : AG7 30) chain C residue 154 type sequence H description binding site for residue EDO C 507 source : AG8 31) chain C residue 203 type sequence D description binding site for residue EDO C 507 source : AG8 32) chain C residue 158 type sequence A description binding site for residue EDO C 508 source : AG9 33) chain C residue 205 type sequence P description binding site for residue EDO C 508 source : AG9 34) chain C residue 342 type sequence R description binding site for residue EDO C 508 source : AG9 35) chain C residue 346 type sequence R description binding site for residue EDO C 508 source : AG9 36) chain C residue 164 type sequence H description binding site for residue ZN C 509 source : AH1 37) chain C residue 200 type sequence H description binding site for residue ZN C 509 source : AH1 38) chain C residue 201 type sequence D description binding site for residue ZN C 509 source : AH1 39) chain C residue 318 type sequence D description binding site for residue ZN C 509 source : AH1 40) chain C residue 273 type sequence M description binding site for residue FFZ C 510 source : AH2 41) chain C residue 319 type sequence L description binding site for residue FFZ C 510 source : AH2 42) chain C residue 321 type sequence N description binding site for residue FFZ C 510 source : AH2 43) chain C residue 336 type sequence I description binding site for residue FFZ C 510 source : AH2 44) chain C residue 368 type sequence S description binding site for residue FFZ C 510 source : AH2 45) chain C residue 369 type sequence Q description binding site for residue FFZ C 510 source : AH2 46) chain C residue 372 type sequence F description binding site for residue FFZ C 510 source : AH2 47) chain C residue 213 type sequence I description binding site for residue PEG C 511 source : AH3 48) chain C residue 225 type sequence D description binding site for residue PEG C 511 source : AH3 49) chain C residue 201 type sequence D description binding site for residue MG C 512 source : AH4 50) chain C residue 349 type sequence E description binding site for residue EDO C 513 source : AH5 51) chain C residue 253 type sequence T description binding site for residue EDO C 514 source : AH6 52) chain C residue 254 type sequence K description binding site for residue EDO C 514 source : AH6 53) chain C residue 231 type sequence N description binding site for residue EDO D 517 source : AJ5 54) chain C residue 234 type sequence L description binding site for residue EDO D 517 source : AJ5 55) chain C residue 160 type ACT_SITE sequence H description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 160 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 57) chain C residue 321 type BINDING sequence N description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 369 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 59) chain C residue 164 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI3 60) chain C residue 200 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 61) chain C residue 318 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 62) chain C residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 63) chain C residue 372 type BINDING sequence F description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5

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