eF-site ID 6nji-AB PDB Code 6nji Chain A, B click to enlarge Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-49 Classification HYDROLASE/HYDROLASE INHIBITOR Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D Source (PDE4D_HUMAN) Sequence A:  EQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIF QERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAA DVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPG VSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENC DIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTM VETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPL QLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVE KSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWY QSTIPQNQVSEFISNTFLD B:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI PQNQVSEFISNTFLD Description Functional site 1) chain A residue 330 type sequence H description binding site for residue ZN A 700 source : AC1 2) chain A residue 366 type sequence H description binding site for residue ZN A 700 source : AC1 3) chain A residue 367 type sequence D description binding site for residue ZN A 700 source : AC1 4) chain A residue 484 type sequence D description binding site for residue ZN A 700 source : AC1 5) chain A residue 367 type sequence D description binding site for residue MG A 701 source : AC2 6) chain A residue 487 type sequence N description binding site for residue KR4 A 702 source : AC3 7) chain A residue 499 type sequence T description binding site for residue KR4 A 702 source : AC3 8) chain A residue 535 type sequence Q description binding site for residue KR4 A 702 source : AC3 9) chain A residue 538 type sequence F description binding site for residue KR4 A 702 source : AC3 10) chain A residue 599 type sequence F description binding site for residue KR4 A 702 source : AC3 11) chain B residue 330 type sequence H description binding site for residue ZN B 700 source : AC4 12) chain B residue 366 type sequence H description binding site for residue ZN B 700 source : AC4 13) chain B residue 367 type sequence D description binding site for residue ZN B 700 source : AC4 14) chain B residue 484 type sequence D description binding site for residue ZN B 700 source : AC4 15) chain B residue 367 type sequence D description binding site for residue MG B 701 source : AC5 16) chain B residue 487 type sequence N description binding site for residue KR4 B 702 source : AC6 17) chain B residue 499 type sequence T description binding site for residue KR4 B 702 source : AC6 18) chain B residue 535 type sequence Q description binding site for residue KR4 B 702 source : AC6 19) chain B residue 538 type sequence F description binding site for residue KR4 B 702 source : AC6 20) chain B residue 599 type sequence F description binding site for residue KR4 B 702 source : AC6 21) chain A residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 23) chain A 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 24) chain A 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 25) chain B 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 26) chain B 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 27) chain A residue 366-377 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 28) chain A residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 29) chain A residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 32) chain A residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 33) chain B 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 A 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 35) chain A 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 36) chain B 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 37) chain B 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 38) chain A residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 39) chain B residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 40) chain A 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 41) chain B 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

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