eF-site ID 6f8u-B PDB Code 6f8u Chain B click to enlarge Title Crystal structure of the PDE4D catalytic domain in complex with GEBR-20b Classification HYDROLASE Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D Source Homo sapiens (Human) (PDE4D_HUMAN) Sequence B:  DVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQER DLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVV QSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSN QFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIF QNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVET KKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLY RQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQ VGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQST IPQAH Description Functional site 1) chain B residue 330 type sequence H description binding site for residue ZN B 601 source : AC7 2) chain B residue 366 type sequence H description binding site for residue ZN B 601 source : AC7 3) chain B residue 367 type sequence D description binding site for residue ZN B 601 source : AC7 4) chain B residue 484 type sequence D description binding site for residue ZN B 601 source : AC7 5) chain B residue 367 type sequence D description binding site for residue MG B 602 source : AC8 6) chain B residue 325 type sequence Y description binding site for residue CZQ B 603 source : AC9 7) chain B residue 439 type sequence M description binding site for residue CZQ B 603 source : AC9 8) chain B residue 487 type sequence N description binding site for residue CZQ B 603 source : AC9 9) chain B residue 495 type sequence Y description binding site for residue CZQ B 603 source : AC9 10) chain B residue 498 type sequence W description binding site for residue CZQ B 603 source : AC9 11) chain B residue 499 type sequence T description binding site for residue CZQ B 603 source : AC9 12) chain B residue 502 type sequence I description binding site for residue CZQ B 603 source : AC9 13) chain B residue 503 type sequence M description binding site for residue CZQ B 603 source : AC9 14) chain B residue 506 type sequence F description binding site for residue CZQ B 603 source : AC9 15) chain B residue 523 type sequence M description binding site for residue CZQ B 603 source : AC9 16) chain B residue 535 type sequence Q description binding site for residue CZQ B 603 source : AC9 17) chain B residue 538 type sequence F description binding site for residue CZQ B 603 source : AC9 18) chain B residue 542 type sequence I description binding site for residue CZQ B 603 source : AC9 19) chain B residue 325 type sequence Y description binding site for residue CZQ B 604 source : AD1 20) chain B residue 374 type sequence S description binding site for residue CZQ B 604 source : AD1 21) chain B residue 487 type sequence N description binding site for residue CZQ B 604 source : AD1 22) chain B residue 488 type sequence P description binding site for residue CZQ B 604 source : AD1 23) chain B residue 495 type sequence Y description binding site for residue CZQ B 604 source : AD1 24) chain B residue 498 type sequence W description binding site for residue CZQ B 604 source : AD1 25) chain B residue 499 type sequence T description binding site for residue CZQ B 604 source : AD1 26) chain B residue 502 type sequence I description binding site for residue CZQ B 604 source : AD1 27) chain B residue 503 type sequence M description binding site for residue CZQ B 604 source : AD1 28) chain B residue 506 type sequence F description binding site for residue CZQ B 604 source : AD1 29) chain B residue 522 type sequence P description binding site for residue CZQ B 604 source : AD1 30) chain B residue 523 type sequence M description binding site for residue CZQ B 604 source : AD1 31) chain B residue 534 type sequence S description binding site for residue CZQ B 604 source : AD1 32) chain B residue 535 type sequence Q description binding site for residue CZQ B 604 source : AD1 33) chain B residue 538 type sequence F description binding site for residue CZQ B 604 source : AD1 34) chain B residue 462 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 462 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 466 type BINDING sequence L 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 37) chain B residue 502 type BINDING sequence I 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 B residue 503 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 39) chain B residue 299 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:21406692 source Swiss-Prot : SWS_FT_FI6 40) chain B residue 301 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:21406692 source Swiss-Prot : SWS_FT_FI6 41) chain B residue 348 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 42) chain B residue 375 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 43) chain B residue 387 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI8

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