eF-site ID 6f8r-B PDB Code 6f8r Chain B click to enlarge Title Crystal structure of the PDE4D catalytic domain in complex with GEBR-54 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 IPQA Description Functional site 1) chain B residue 325 type sequence Y description binding site for residue CZK B 601 source : AC6 2) chain B residue 439 type sequence M description binding site for residue CZK B 601 source : AC6 3) chain B residue 487 type sequence N description binding site for residue CZK B 601 source : AC6 4) chain B residue 503 type sequence M description binding site for residue CZK B 601 source : AC6 5) chain B residue 523 type sequence M description binding site for residue CZK B 601 source : AC6 6) chain B residue 534 type sequence S description binding site for residue CZK B 601 source : AC6 7) chain B residue 535 type sequence Q description binding site for residue CZK B 601 source : AC6 8) chain B residue 538 type sequence F description binding site for residue CZK B 601 source : AC6 9) chain B residue 367 type sequence D description binding site for residue MG B 602 source : AC7 10) chain B residue 330 type sequence H description binding site for residue ZN B 603 source : AC8 11) chain B residue 366 type sequence H description binding site for residue ZN B 603 source : AC8 12) chain B residue 367 type sequence D description binding site for residue ZN B 603 source : AC8 13) chain B residue 484 type sequence D description binding site for residue ZN B 603 source : AC8 14) chain B residue 428 type sequence K description binding site for residue EDO B 604 source : AC9 15) chain B residue 431 type sequence I description binding site for residue EDO B 604 source : AC9 16) chain B residue 432 type sequence D description binding site for residue EDO B 604 source : AC9 17) chain B residue 299 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:21406692 source Swiss-Prot : SWS_FT_FI6 18) chain B residue 301 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:21406692 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 348 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 20) chain B residue 375 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 21) 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 22) chain B residue 462 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 23) 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 24) 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 25) 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 26) chain B 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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