eF-site ID 1ro9-A PDB Code 1ro9 Chain A click to enlarge Title CRYSTAL STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHODIESTERASE 4B2B COMPLEXED WITH 8-Br-AMP Classification HYDROLASE Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4B Source Homo sapiens (Human) (PDE4B_HUMAN) Sequence A:  SISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRP LTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDV AYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAA AIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVG FKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHM SLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCA DLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPM CDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILD TLEDNRNWYQSMIPQAPA Description Functional site 1) chain A residue 238 type sequence H description BINDING SITE FOR RESIDUE ZN A 529 source : AC1 2) chain A residue 274 type sequence H description BINDING SITE FOR RESIDUE ZN A 529 source : AC1 3) chain A residue 275 type sequence D description BINDING SITE FOR RESIDUE ZN A 529 source : AC1 4) chain A residue 392 type sequence D description BINDING SITE FOR RESIDUE ZN A 529 source : AC1 5) chain A residue 275 type sequence D description BINDING SITE FOR RESIDUE ZN A 530 source : AC2 6) chain A residue 233 type sequence Y description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 7) chain A residue 234 type sequence H description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 8) chain A residue 392 type sequence D description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 9) chain A residue 393 type sequence L description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 10) chain A residue 395 type sequence N description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 11) chain A residue 403 type sequence Y description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 12) chain A residue 414 type sequence F description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 13) chain A residue 443 type sequence Q description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 14) chain A residue 446 type sequence F description BINDING SITE FOR RESIDUE 8BR A 531 source : AC5 15) chain A residue 234 type ACT_SITE sequence H description Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR source Swiss-Prot : SWS_FT_FI1 16) chain A residue 234 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 443 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 274-285 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 19) chain A residue 487 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P14646 source Swiss-Prot : SWS_FT_FI8 20) chain A residue 489 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P14646 source Swiss-Prot : SWS_FT_FI8 21) chain A residue 238 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P source Swiss-Prot : SWS_FT_FI3 22) chain A residue 274 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P source Swiss-Prot : SWS_FT_FI4 23) chain A residue 275 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR source Swiss-Prot : SWS_FT_FI5 24) chain A residue 392 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:3D3P source Swiss-Prot : SWS_FT_FI6 25) chain A residue 446 type BINDING sequence F description BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5 source Swiss-Prot : SWS_FT_FI7

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