eF-site ID 6njj-C PDB Code 6njj Chain C 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 C:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQ LYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEK SQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQ STIPNQVSEFISNTFLD Description Functional site 1) chain C residue 320 type sequence H description binding site for residue BTB A 704 source : AC4 2) chain C residue 322 type sequence D description binding site for residue BTB A 704 source : AC4 3) chain C residue 369 type sequence D description binding site for residue BTB A 704 source : AC4 4) chain C residue 371 type sequence P description binding site for residue BTB A 704 source : AC4 5) chain C residue 512 type sequence R description binding site for residue BTB A 704 source : AC4 6) chain C residue 330 type sequence H description binding site for residue ZN C 701 source : AD3 7) chain C residue 366 type sequence H description binding site for residue ZN C 701 source : AD3 8) chain C residue 367 type sequence D description binding site for residue ZN C 701 source : AD3 9) chain C residue 484 type sequence D description binding site for residue ZN C 701 source : AD3 10) chain C residue 367 type sequence D description binding site for residue MG C 702 source : AD4 11) chain C residue 325 type sequence Y description binding site for residue KR7 C 703 source : AD5 12) chain C residue 439 type sequence M description binding site for residue KR7 C 703 source : AD5 13) chain C residue 487 type sequence N description binding site for residue KR7 C 703 source : AD5 14) chain C residue 495 type sequence Y description binding site for residue KR7 C 703 source : AD5 15) chain C residue 498 type sequence W description binding site for residue KR7 C 703 source : AD5 16) chain C residue 499 type sequence T description binding site for residue KR7 C 703 source : AD5 17) chain C residue 502 type sequence I description binding site for residue KR7 C 703 source : AD5 18) chain C residue 535 type sequence Q description binding site for residue KR7 C 703 source : AD5 19) chain C residue 538 type sequence F description binding site for residue KR7 C 703 source : AD5 20) chain C residue 599 type sequence F description binding site for residue KR7 C 703 source : AD5 21) chain C residue 271 type sequence H description binding site for residue SO4 C 704 source : AD6 22) chain C residue 272 type sequence V description binding site for residue SO4 C 704 source : AD6 23) chain C residue 273 type sequence F description binding site for residue SO4 C 704 source : AD6 24) chain C residue 274 type sequence R description binding site for residue SO4 C 704 source : AD6 25) chain C residue 493 type sequence Q description binding site for residue SO4 C 704 source : AD6 26) chain C residue 494 type sequence L description binding site for residue SO4 C 704 source : AD6 27) chain C residue 497 type sequence Q description binding site for residue SO4 C 704 source : AD6 28) chain C residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 29) chain C 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 C 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 C residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 32) chain C residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 33) chain C residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 34) chain C 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 35) chain C 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 36) chain C 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 37) chain C residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5

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