eF-site ID 5ae0-A PDB Code 5ae0 Chain A click to enlarge Title Perdeuterated mouse CNPase catalytic domain at atomic resolution Classification HYDROLASE Compound 2', 3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE Source (CN37_MOUSE) Sequence A:  KDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKE LRHFISGDEPKEKLELVSYFGKRPPGVLHCTTKFCDYGKA AGAEEYAQQEVVKRSYGKAFKLSISALFVTPKTAGAQVVL TDQELQLWPSDLDKPSASEGLPPGSRAHVTLGCAADVQPV QTGLDLLDILQQVKGGSQGEAVGELPRGKLYSLGKGRWML SLTKKMEVKAIFTGYYG Description Functional site 1) chain A residue 195 type sequence H description BINDING SITE FOR RESIDUE CIT A 1379 source : AC1 2) chain A residue 196 type sequence K description BINDING SITE FOR RESIDUE CIT A 1379 source : AC1 3) chain A residue 344 type sequence G description BINDING SITE FOR RESIDUE CIT A 1379 source : AC1 4) chain A residue 345 type sequence E description BINDING SITE FOR RESIDUE CIT A 1379 source : AC1 5) chain A residue 305 type sequence G description BINDING SITE FOR RESIDUE CL A 1380 source : AC2 6) chain A residue 306 type sequence S description BINDING SITE FOR RESIDUE CL A 1380 source : AC2 7) chain A residue 307 type sequence R description BINDING SITE FOR RESIDUE CL A 1380 source : AC2 8) chain A residue 230 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:22393399 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 309 type ACT_SITE sequence H description Proton donor => ECO:0000269|PubMed:22393399 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13233 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 219 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13233 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 338 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13233 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 232 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 14) chain A residue 311 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3

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