eF-site ID 6hwo-A PDB Code 6hwo Chain A 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 A:  GVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIM HTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNN IHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDV DHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQ EENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLAD LKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNP TKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHN ASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDN REWYQST Description Functional site 1) chain A residue 262 type sequence K description binding site for residue EDO A 501 source : AC1 2) chain A residue 266 type sequence D description binding site for residue EDO A 501 source : AC1 3) chain A residue 238 type sequence F description binding site for residue EDO A 502 source : AC2 4) chain A residue 249 type sequence F description binding site for residue EDO A 502 source : AC2 5) chain A residue 257 type sequence R description binding site for residue EDO A 502 source : AC2 6) chain A residue 156 type sequence D description binding site for residue EDO A 503 source : AC3 7) chain A residue 157 type sequence V description binding site for residue EDO A 503 source : AC3 8) chain A residue 158 type sequence A description binding site for residue EDO A 503 source : AC3 9) chain A residue 205 type sequence P description binding site for residue EDO A 503 source : AC3 10) chain A residue 346 type sequence R description binding site for residue EDO A 503 source : AC3 11) chain A residue 251 type sequence N description binding site for residue EDO A 504 source : AC4 12) chain A residue 252 type sequence L description binding site for residue EDO A 504 source : AC4 13) chain A residue 135 type sequence F description binding site for residue EDO A 505 source : AC5 14) chain A residue 256 type sequence Q description binding site for residue EDO A 505 source : AC5 15) chain A residue 134 type sequence T description binding site for residue EDO A 506 source : AC6 16) chain A residue 136 type sequence K description binding site for residue EDO A 506 source : AC6 17) chain A residue 175 type sequence L description binding site for residue EDO A 507 source : AC7 18) chain A residue 178 type sequence T description binding site for residue EDO A 507 source : AC7 19) chain A residue 384 type sequence W description binding site for residue EDO A 507 source : AC7 20) chain A residue 388 type sequence V description binding site for residue EDO A 507 source : AC7 21) chain A residue 266 type sequence D description binding site for residue EDO A 508 source : AC8 22) chain A residue 311 type sequence Q description binding site for residue EDO A 508 source : AC8 23) chain A residue 132 type sequence L description binding site for residue PEG A 509 source : AC9 24) chain A residue 136 type sequence K description binding site for residue PEG A 509 source : AC9 25) chain A residue 137 type sequence I description binding site for residue PEG A 509 source : AC9 26) chain A residue 164 type sequence H description binding site for residue ZN A 510 source : AD1 27) chain A residue 200 type sequence H description binding site for residue ZN A 510 source : AD1 28) chain A residue 201 type sequence D description binding site for residue ZN A 510 source : AD1 29) chain A residue 318 type sequence D description binding site for residue ZN A 510 source : AD1 30) chain A residue 152 type sequence H description binding site for residue EDO A 511 source : AD2 31) chain A residue 243 type sequence E description binding site for residue EDO A 511 source : AD2 32) chain A residue 186 type sequence T description binding site for residue EDO A 512 source : AD3 33) chain A residue 189 type sequence E description binding site for residue EDO A 512 source : AD3 34) chain A residue 259 type sequence S description binding site for residue EDO A 512 source : AD3 35) chain A residue 263 type sequence M description binding site for residue EDO A 512 source : AD3 36) chain A residue 273 type sequence M description binding site for residue FFZ A 513 source : AD4 37) chain A residue 319 type sequence L description binding site for residue FFZ A 513 source : AD4 38) chain A residue 336 type sequence I description binding site for residue FFZ A 513 source : AD4 39) chain A residue 337 type sequence M description binding site for residue FFZ A 513 source : AD4 40) chain A residue 357 type sequence M description binding site for residue FFZ A 513 source : AD4 41) chain A residue 368 type sequence S description binding site for residue FFZ A 513 source : AD4 42) chain A residue 369 type sequence Q description binding site for residue FFZ A 513 source : AD4 43) chain A residue 372 type sequence F description binding site for residue FFZ A 513 source : AD4 44) chain A residue 376 type sequence I description binding site for residue FFZ A 513 source : AD4 45) chain A residue 201 type sequence D description binding site for residue MG A 514 source : AD5 46) chain A residue 243 type sequence E description binding site for residue EDO A 515 source : AD6 47) chain A residue 244 type sequence E description binding site for residue EDO A 515 source : AD6 48) chain A residue 245 type sequence N description binding site for residue EDO A 515 source : AD6 49) chain A residue 218 type sequence E description binding site for residue EDO A 516 source : AD7 50) chain A residue 140 type sequence D description binding site for residue EDO A 517 source : AD8 51) chain A residue 141 type sequence T description binding site for residue EDO A 517 source : AD8 52) chain A residue 245 type sequence N description binding site for residue EDO A 517 source : AD8 53) chain A residue 210 type sequence Q description binding site for residue EDO A 518 source : AD9 54) chain A residue 213 type sequence I description binding site for residue EDO A 518 source : AD9 55) chain A residue 289 type sequence T description binding site for residue EDO A 519 source : AE1 56) chain A residue 291 type sequence K description binding site for residue EDO A 519 source : AE1 57) chain A residue 298 type sequence L description binding site for residue EDO A 519 source : AE1 58) chain A residue 299 type sequence L description binding site for residue EDO A 519 source : AE1 59) chain A residue 105 type sequence H description binding site for residue EPE A 520 source : AE2 60) chain A residue 106 type sequence V description binding site for residue EPE A 520 source : AE2 61) chain A residue 107 type sequence F description binding site for residue EPE A 520 source : AE2 62) chain A residue 108 type sequence R description binding site for residue EPE A 520 source : AE2 63) chain A residue 111 type sequence E description binding site for residue EPE A 520 source : AE2 64) chain A residue 328 type sequence L description binding site for residue EPE A 520 source : AE2 65) chain A residue 331 type sequence Q description binding site for residue EPE A 520 source : AE2 66) chain A residue 115 type sequence N description binding site for residue PEG A 521 source : AE3 67) chain A residue 116 type sequence R description binding site for residue PEG A 521 source : AE3 68) chain A residue 150 type sequence E description binding site for residue PEG A 521 source : AE3 69) chain A residue 151 type sequence D description binding site for residue PEG A 521 source : AE3 70) chain A residue 153 type sequence Y description binding site for residue PEG A 521 source : AE3 71) chain A residue 154 type sequence H description binding site for residue PEG A 521 source : AE3 72) chain A residue 155 type sequence A description binding site for residue PEG A 521 source : AE3 73) chain A residue 225 type sequence D description binding site for residue EDO B 514 source : AF8 74) chain A residue 244 type sequence E description binding site for residue EDO C 501 source : AG2 75) chain A residue 342 type sequence R description binding site for residue EDO C 502 source : AG3 76) chain A residue 140 type sequence D description binding site for residue EDO C 513 source : AH5 77) chain A residue 143 type sequence I description binding site for residue EDO C 513 source : AH5 78) chain A residue 188 type sequence L description binding site for residue EDO D 501 source : AH7 79) chain A residue 255 type sequence K description binding site for residue EDO D 501 source : AH7 80) chain A residue 256 type sequence Q description binding site for residue EDO D 501 source : AH7 81) chain A residue 134 type sequence T description binding site for residue EDO D 504 source : AI1 82) chain A residue 251 type sequence N description binding site for residue EDO D 504 source : AI1 83) chain A residue 256 type sequence Q description binding site for residue EDO D 504 source : AI1 84) chain A residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 85) chain A residue 372 type BINDING sequence F description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 86) chain A residue 160 type ACT_SITE sequence H description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 87) chain A 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 88) chain A 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 89) chain A 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 90) chain A residue 200-211 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 91) chain A 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 92) chain A 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 93) chain A 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 94) chain A residue 85 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI6

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