eF-site ID 2yph-A PDB Code 2yph Chain A click to enlarge Title Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H230S, crystallized with 2',3-(RP)- cyclic-AMPS Classification HYDROLASE Compound 2', 3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE Source (CN37_MOUSE) Sequence A:  DFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKEL RHFISGEKLELVSYFGKRPPGVLSCTTKFCDYGKAAGAEE YAQQEVVKRSYGKAFKLSISALFVTPKTAGAQVVLTDQEL QLWPSDLDKPSASEGLPPGSRAHVTLGCAADVQPVQTGLD LLDILQQVKGGSQGEAVGELPRGKLYSLGKGRWMLSLTKK MEVKAIFTGYYG Description Functional site 1) chain A residue 223 type sequence K description BINDING SITE FOR RESIDUE ACT A 1379 source : AC1 2) chain A residue 224 type sequence R description BINDING SITE FOR RESIDUE ACT A 1379 source : AC1 3) chain A residue 225 type sequence P description BINDING SITE FOR RESIDUE ACT A 1379 source : AC1 4) chain A residue 314 type sequence C description BINDING SITE FOR RESIDUE ACT A 1379 source : AC1 5) chain A residue 273 type sequence K description BINDING SITE FOR RESIDUE CL A 1380 source : AC2 6) chain A residue 168 type sequence Y description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 7) chain A residue 232 type sequence T description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 8) chain A residue 235 type sequence F description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 9) chain A residue 309 type sequence H description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 10) chain A residue 311 type sequence T description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 11) chain A residue 320 type sequence P description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 12) chain A residue 321 type sequence V description BINDING SITE FOR RESIDUE QQY A 1381 source : AC3 13) chain A residue 250 type ACT_SITE sequence Q description Proton acceptor => ECO:0000269|PubMed:22393399 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 329 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:22393399 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 252 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 16) chain A residue 331 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 17) chain A residue 169 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 227 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P13233 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 239 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P13233 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 358 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P13233 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links