eF-site ID 6f8u-A PDB Code 6f8u Chain A 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 A:  DVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQER DLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVV QSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSN QFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIF QNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVET KKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLY RQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQ VGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQST IP Description Functional site 1) chain A residue 330 type sequence H description binding site for residue ZN A 601 source : AC1 2) chain A residue 366 type sequence H description binding site for residue ZN A 601 source : AC1 3) chain A residue 367 type sequence D description binding site for residue ZN A 601 source : AC1 4) chain A residue 484 type sequence D description binding site for residue ZN A 601 source : AC1 5) chain A residue 367 type sequence D description binding site for residue MG A 602 source : AC2 6) chain A residue 467 type sequence D description binding site for residue MG A 604 source : AC4 7) chain A residue 471 type sequence D description binding site for residue MG A 604 source : AC4 8) chain A residue 527 type sequence H description binding site for residue MG A 604 source : AC4 9) chain A residue 374 type sequence S description binding site for residue CZQ A 606 source : AC6 10) chain A residue 487 type sequence N description binding site for residue CZQ A 606 source : AC6 11) chain A residue 488 type sequence P description binding site for residue CZQ A 606 source : AC6 12) chain A residue 495 type sequence Y description binding site for residue CZQ A 606 source : AC6 13) chain A residue 498 type sequence W description binding site for residue CZQ A 606 source : AC6 14) chain A residue 499 type sequence T description binding site for residue CZQ A 606 source : AC6 15) chain A residue 502 type sequence I description binding site for residue CZQ A 606 source : AC6 16) chain A residue 506 type sequence F description binding site for residue CZQ A 606 source : AC6 17) chain A residue 509 type sequence Q description binding site for residue CZQ A 606 source : AC6 18) chain A residue 522 type sequence P description binding site for residue CZQ A 606 source : AC6 19) chain A residue 523 type sequence M description binding site for residue CZQ A 606 source : AC6 20) chain A residue 535 type sequence Q description binding site for residue CZQ A 606 source : AC6 21) chain A residue 538 type sequence F description binding site for residue CZQ A 606 source : AC6 22) chain A 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 23) chain A residue 462 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 299 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:21406692 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 301 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:21406692 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 348 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 375 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 387 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI8 29) chain A residue 366-377 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 30) chain A 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 31) chain A 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 32) chain A residue 503 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5

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