eF-site ID 6njh-C PDB Code 6njh Chain C click to enlarge Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-48 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 318 type sequence H description binding site for residue MG A 704 source : AC4 2) chain C residue 330 type sequence H description binding site for residue ZN C 700 source : AC8 3) chain C residue 366 type sequence H description binding site for residue ZN C 700 source : AC8 4) chain C residue 367 type sequence D description binding site for residue ZN C 700 source : AC8 5) chain C residue 484 type sequence D description binding site for residue ZN C 700 source : AC8 6) chain C residue 367 type sequence D description binding site for residue MG C 701 source : AC9 7) chain C residue 326 type sequence H description binding site for residue KRD C 702 source : AD1 8) chain C residue 487 type sequence N description binding site for residue KRD C 702 source : AD1 9) chain C residue 499 type sequence T description binding site for residue KRD C 702 source : AD1 10) chain C residue 502 type sequence I description binding site for residue KRD C 702 source : AD1 11) chain C residue 506 type sequence F description binding site for residue KRD C 702 source : AD1 12) chain C residue 523 type sequence M description binding site for residue KRD C 702 source : AD1 13) chain C residue 535 type sequence Q description binding site for residue KRD C 702 source : AD1 14) chain C residue 538 type sequence F description binding site for residue KRD C 702 source : AD1 15) chain C residue 599 type sequence F description binding site for residue KRD C 702 source : AD1 16) chain C residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 17) chain C residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 18) chain C residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 19) 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 20) 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 21) 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 22) chain C residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 23) 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 24) 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 25) 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

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