eF-site ID 6njj-A PDB Code 6njj Chain A click to enlarge Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with BPN14770 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 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 325 type sequence Y description binding site for residue KR7 A 703 source : AC3 7) chain A residue 439 type sequence M description binding site for residue KR7 A 703 source : AC3 8) chain A residue 487 type sequence N description binding site for residue KR7 A 703 source : AC3 9) chain A residue 495 type sequence Y description binding site for residue KR7 A 703 source : AC3 10) chain A residue 498 type sequence W description binding site for residue KR7 A 703 source : AC3 11) chain A residue 499 type sequence T description binding site for residue KR7 A 703 source : AC3 12) chain A residue 502 type sequence I description binding site for residue KR7 A 703 source : AC3 13) chain A residue 535 type sequence Q description binding site for residue KR7 A 703 source : AC3 14) chain A residue 538 type sequence F description binding site for residue KR7 A 703 source : AC3 15) chain A residue 599 type sequence F description binding site for residue KR7 A 703 source : AC3 16) chain A residue 603 type sequence T description binding site for residue KR7 A 703 source : AC3 17) chain A residue 318 type sequence H description binding site for residue BTB A 704 source : AC4 18) chain A residue 409 type sequence E description binding site for residue BTB A 704 source : AC4 19) chain A residue 318 type sequence H description binding site for residue ZN A 705 source : AC5 20) chain A residue 271 type sequence H description binding site for residue SO4 A 706 source : AC6 21) chain A residue 272 type sequence V description binding site for residue SO4 A 706 source : AC6 22) chain A residue 273 type sequence F description binding site for residue SO4 A 706 source : AC6 23) chain A residue 274 type sequence R description binding site for residue SO4 A 706 source : AC6 24) chain A residue 494 type sequence L description binding site for residue SO4 A 706 source : AC6 25) chain A residue 497 type sequence Q description binding site for residue SO4 A 706 source : AC6 26) chain A residue 341 type sequence L description binding site for residue EDO A 707 source : AC7 27) chain A residue 344 type sequence T description binding site for residue EDO A 707 source : AC7 28) chain A residue 550 type sequence W description binding site for residue EDO A 707 source : AC7 29) chain A residue 557 type sequence D description binding site for residue EDO A 707 source : AC7 30) chain A residue 561 type sequence I description binding site for residue EDO A 707 source : AC7 31) chain A residue 366-377 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 32) chain A residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 33) 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 34) 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 35) 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 36) 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 37) 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 38) chain A residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 39) chain A residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 40) chain A residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 41) 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

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