eF-site ID 6njj-B PDB Code 6njj Chain B 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 B:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI PNQVSEFISNTFLD Description Functional site 1) chain B residue 330 type sequence H description binding site for residue ZN B 701 source : AC8 2) chain B residue 366 type sequence H description binding site for residue ZN B 701 source : AC8 3) chain B residue 367 type sequence D description binding site for residue ZN B 701 source : AC8 4) chain B residue 484 type sequence D description binding site for residue ZN B 701 source : AC8 5) chain B residue 367 type sequence D description binding site for residue MG B 702 source : AC9 6) chain B residue 325 type sequence Y description binding site for residue KR7 B 703 source : AD1 7) chain B residue 439 type sequence M description binding site for residue KR7 B 703 source : AD1 8) chain B residue 487 type sequence N description binding site for residue KR7 B 703 source : AD1 9) chain B residue 495 type sequence Y description binding site for residue KR7 B 703 source : AD1 10) chain B residue 498 type sequence W description binding site for residue KR7 B 703 source : AD1 11) chain B residue 499 type sequence T description binding site for residue KR7 B 703 source : AD1 12) chain B residue 502 type sequence I description binding site for residue KR7 B 703 source : AD1 13) chain B residue 535 type sequence Q description binding site for residue KR7 B 703 source : AD1 14) chain B residue 538 type sequence F description binding site for residue KR7 B 703 source : AD1 15) chain B residue 599 type sequence F description binding site for residue KR7 B 703 source : AD1 16) chain B residue 271 type sequence H description binding site for residue SO4 B 704 source : AD2 17) chain B residue 272 type sequence V description binding site for residue SO4 B 704 source : AD2 18) chain B residue 273 type sequence F description binding site for residue SO4 B 704 source : AD2 19) chain B residue 274 type sequence R description binding site for residue SO4 B 704 source : AD2 20) chain B residue 493 type sequence Q description binding site for residue SO4 B 704 source : AD2 21) chain B residue 494 type sequence L description binding site for residue SO4 B 704 source : AD2 22) chain B residue 497 type sequence Q description binding site for residue SO4 B 704 source : AD2 23) chain B residue 320 type sequence H description binding site for residue BTB D 704 source : AE1 24) chain B residue 322 type sequence D description binding site for residue BTB D 704 source : AE1 25) chain B residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 26) 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 27) 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 28) 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 29) 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 30) 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 31) chain B residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 32) chain B residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 33) chain B residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 34) 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

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