eF-site ID 6ink-AB PDB Code 6ink Chain A, B click to enlarge Title Crystal structure of PDE4D complexed with a novel inhibitor Classification HYDROLASE/HYDROLASE INHIBITOR Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D Source (PDE4D_HUMAN) Sequence A:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQ LYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEK SQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQ STI B:  VLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERD LLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQ STHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQ FLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQ NLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETK KVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWT DRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFI DYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIP Description Functional site 1) chain A residue 164 type sequence H description binding site for residue ZN A 501 source : AC1 2) chain A residue 200 type sequence H description binding site for residue ZN A 501 source : AC1 3) chain A residue 201 type sequence D description binding site for residue ZN A 501 source : AC1 4) chain A residue 318 type sequence D description binding site for residue ZN A 501 source : AC1 5) chain A residue 201 type sequence D description binding site for residue MG A 502 source : AC2 6) chain A residue 159 type sequence Y description binding site for residue AKU A 503 source : AC3 7) chain A residue 160 type sequence H description binding site for residue AKU A 503 source : AC3 8) chain A residue 321 type sequence N description binding site for residue AKU A 503 source : AC3 9) chain A residue 336 type sequence I description binding site for residue AKU A 503 source : AC3 10) chain A residue 357 type sequence M description binding site for residue AKU A 503 source : AC3 11) chain A residue 369 type sequence Q description binding site for residue AKU A 503 source : AC3 12) chain A residue 372 type sequence F description binding site for residue AKU A 503 source : AC3 13) chain A residue 208 type sequence S description binding site for residue EDO A 504 source : AC4 14) chain A residue 340 type sequence F description binding site for residue EDO A 504 source : AC4 15) chain A residue 356 type sequence P description binding site for residue EDO A 504 source : AC4 16) chain A residue 262 type sequence K description binding site for residue EDO A 505 source : AC5 17) chain A residue 265 type sequence I description binding site for residue EDO A 505 source : AC5 18) chain A residue 266 type sequence D description binding site for residue EDO A 505 source : AC5 19) chain B residue 164 type sequence H description binding site for residue ZN B 501 source : AC6 20) chain B residue 200 type sequence H description binding site for residue ZN B 501 source : AC6 21) chain B residue 201 type sequence D description binding site for residue ZN B 501 source : AC6 22) chain B residue 318 type sequence D description binding site for residue ZN B 501 source : AC6 23) chain B residue 201 type sequence D description binding site for residue MG B 502 source : AC7 24) chain B residue 159 type sequence Y description binding site for residue AKU B 503 source : AC8 25) chain B residue 160 type sequence H description binding site for residue AKU B 503 source : AC8 26) chain B residue 321 type sequence N description binding site for residue AKU B 503 source : AC8 27) chain B residue 336 type sequence I description binding site for residue AKU B 503 source : AC8 28) chain B residue 357 type sequence M description binding site for residue AKU B 503 source : AC8 29) chain B residue 369 type sequence Q description binding site for residue AKU B 503 source : AC8 30) chain B residue 372 type sequence F description binding site for residue AKU B 503 source : AC8 31) chain B residue 208 type sequence S description binding site for residue EDO B 504 source : AC9 32) chain B residue 340 type sequence F description binding site for residue EDO B 504 source : AC9 33) chain B residue 356 type sequence P description binding site for residue EDO B 504 source : AC9 34) chain A residue 224 type sequence N description binding site for residue EDO B 505 source : AD1 35) chain B residue 262 type sequence K description binding site for residue EDO B 505 source : AD1 36) chain B residue 265 type sequence I description binding site for residue EDO B 505 source : AD1 37) chain B residue 266 type sequence D description binding site for residue EDO B 505 source : AD1 38) chain A residue 200-211 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 39) chain A residue 160 type ACT_SITE sequence H description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 160 type ACT_SITE sequence H description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 41) 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 42) 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 43) 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 44) chain B 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 45) chain B 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 46) chain B 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 47) 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 48) chain B 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 49) 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 50) 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 51) chain B 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 52) chain B 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 53) chain A residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 54) chain A residue 372 type BINDING sequence F description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 55) chain B residue 201 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 56) chain B residue 372 type BINDING sequence F description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5

Display surface Download Links