eF-site ID 6njh-ABCD PDB Code 6njh Chain A, B, C, D click to enlarge Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-48 Classification HYDROLASE/HYDROLASE INHIBITOR Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D Source (PDE4D_HUMAN) Sequence A:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI PNQVSEFISNTFLD B:  EQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIF QERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAA DVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPG VSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENC DIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTM VETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLY RQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQ VGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQST IPNQVSEFISNTFLD C:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQ LYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEK SQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQ STIPNQVSEFISNTFLD D:  EDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQE RDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADV VQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVS NQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDI FQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVE TKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQ WTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVG FIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIP NQVSEFISNTFLD Description Functional site 1) chain A residue 330 type sequence H description binding site for residue ZN A 701 source : AC1 2) chain A residue 366 type sequence H description binding site for residue ZN A 701 source : AC1 3) chain A residue 367 type sequence D description binding site for residue ZN A 701 source : AC1 4) chain A residue 484 type sequence D description binding site for residue ZN A 701 source : AC1 5) chain A residue 367 type sequence D description binding site for residue MG A 702 source : AC2 6) chain A residue 326 type sequence H description binding site for residue KRD A 703 source : AC3 7) chain A residue 487 type sequence N description binding site for residue KRD A 703 source : AC3 8) chain A residue 499 type sequence T description binding site for residue KRD A 703 source : AC3 9) chain A residue 506 type sequence F description binding site for residue KRD A 703 source : AC3 10) chain A residue 535 type sequence Q description binding site for residue KRD A 703 source : AC3 11) chain A residue 538 type sequence F description binding site for residue KRD A 703 source : AC3 12) chain A residue 599 type sequence F description binding site for residue KRD A 703 source : AC3 13) chain A residue 384 type sequence E description binding site for residue MG A 704 source : AC4 14) chain C residue 318 type sequence H description binding site for residue MG A 704 source : AC4 15) chain B residue 330 type sequence H description binding site for residue ZN B 701 source : AC5 16) chain B residue 366 type sequence H description binding site for residue ZN B 701 source : AC5 17) chain B residue 367 type sequence D description binding site for residue ZN B 701 source : AC5 18) chain B residue 484 type sequence D description binding site for residue ZN B 701 source : AC5 19) chain B residue 367 type sequence D description binding site for residue MG B 702 source : AC6 20) chain B residue 326 type sequence H description binding site for residue KRD B 703 source : AC7 21) chain B residue 487 type sequence N description binding site for residue KRD B 703 source : AC7 22) chain B residue 498 type sequence W description binding site for residue KRD B 703 source : AC7 23) chain B residue 499 type sequence T description binding site for residue KRD B 703 source : AC7 24) chain B residue 502 type sequence I description binding site for residue KRD B 703 source : AC7 25) chain B residue 506 type sequence F description binding site for residue KRD B 703 source : AC7 26) chain B residue 523 type sequence M description binding site for residue KRD B 703 source : AC7 27) chain B residue 535 type sequence Q description binding site for residue KRD B 703 source : AC7 28) chain B residue 538 type sequence F description binding site for residue KRD B 703 source : AC7 29) chain B residue 599 type sequence F description binding site for residue KRD B 703 source : AC7 30) chain B residue 600 type sequence I description binding site for residue KRD B 703 source : AC7 31) chain C residue 330 type sequence H description binding site for residue ZN C 700 source : AC8 32) chain C residue 366 type sequence H description binding site for residue ZN C 700 source : AC8 33) chain C residue 367 type sequence D description binding site for residue ZN C 700 source : AC8 34) chain C residue 484 type sequence D description binding site for residue ZN C 700 source : AC8 35) chain C residue 367 type sequence D description binding site for residue MG C 701 source : AC9 36) chain C residue 326 type sequence H description binding site for residue KRD C 702 source : AD1 37) chain C residue 487 type sequence N description binding site for residue KRD C 702 source : AD1 38) chain C residue 499 type sequence T description binding site for residue KRD C 702 source : AD1 39) chain C residue 502 type sequence I description binding site for residue KRD C 702 source : AD1 40) chain C residue 506 type sequence F description binding site for residue KRD C 702 source : AD1 41) chain C residue 523 type sequence M description binding site for residue KRD C 702 source : AD1 42) chain C residue 535 type sequence Q description binding site for residue KRD C 702 source : AD1 43) chain C residue 538 type sequence F description binding site for residue KRD C 702 source : AD1 44) chain C residue 599 type sequence F description binding site for residue KRD C 702 source : AD1 45) chain B residue 318 type sequence H description binding site for residue MG D 701 source : AD2 46) chain D residue 384 type sequence E description binding site for residue MG D 701 source : AD2 47) chain D residue 330 type sequence H description binding site for residue ZN D 702 source : AD3 48) chain D residue 366 type sequence H description binding site for residue ZN D 702 source : AD3 49) chain D residue 367 type sequence D description binding site for residue ZN D 702 source : AD3 50) chain D residue 484 type sequence D description binding site for residue ZN D 702 source : AD3 51) chain D residue 367 type sequence D description binding site for residue MG D 703 source : AD4 52) chain D residue 326 type sequence H description binding site for residue KRD D 704 source : AD5 53) chain D residue 374 type sequence S description binding site for residue KRD D 704 source : AD5 54) chain D residue 487 type sequence N description binding site for residue KRD D 704 source : AD5 55) chain D residue 498 type sequence W description binding site for residue KRD D 704 source : AD5 56) chain D residue 499 type sequence T description binding site for residue KRD D 704 source : AD5 57) chain D residue 523 type sequence M description binding site for residue KRD D 704 source : AD5 58) chain D residue 535 type sequence Q description binding site for residue KRD D 704 source : AD5 59) chain D residue 538 type sequence F description binding site for residue KRD D 704 source : AD5 60) chain D residue 599 type sequence F description binding site for residue KRD D 704 source : AD5 61) chain A residue 366-377 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 62) chain A residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 63) chain B residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 64) chain C residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 65) chain D residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 72) chain D residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 73) chain D residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 391 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:2PW3 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 391 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:2PW3 source Swiss-Prot : SWS_FT_FI3 76) chain C residue 391 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:2PW3 source Swiss-Prot : SWS_FT_FI3 77) chain D residue 391 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:2PW3 source Swiss-Prot : SWS_FT_FI3 78) chain A residue 427 type BINDING sequence R 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 79) chain A residue 545 type BINDING sequence P 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 80) chain B residue 427 type BINDING sequence R 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 81) chain B residue 545 type BINDING sequence P 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 82) chain C residue 427 type BINDING sequence R 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 83) chain C residue 545 type BINDING sequence P 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 84) chain D residue 427 type BINDING sequence R 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 85) chain D residue 545 type BINDING sequence P 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 86) chain A residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 87) chain B residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 88) chain C residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 89) chain D residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 90) chain A residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 91) chain A residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 92) chain B residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 93) chain B residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 94) chain C residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 95) chain C residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 96) chain D residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 97) chain D residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 98) chain A residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 99) chain B residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 100) chain C residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 101) chain D residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7

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