eF-site ID 5n3m-A PDB Code 5n3m Chain A click to enlarge Title cAMP-dependent Protein Kinase A from Cricetulus griseus in complex with fragment like molecule D-arginine Classification TRANSFERASE Compound cAMP-dependent protein kinase catalytic subunit alpha Source (KAPCA_CRIGR) Sequence A:  EQESVKEFLAKAKEEFLKKWESPSQNTAQLDHFDRIKTLG TGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLN EKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFS HLRRIGRFXEPHARFYAAQIVLTFEYLHSLDLIYRDLKPE NLLIDQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEII LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI VSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVND IKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDY EEEEIRVXINEKCGKEFTEF Description Functional site 1) chain A residue 15 type sequence V description binding site for residue MPD A 401 source : AC1 2) chain A residue 152 type sequence L description binding site for residue MPD A 401 source : AC1 3) chain A residue 155 type sequence E description binding site for residue MPD A 401 source : AC1 4) chain A residue 306 type sequence Y description binding site for residue MPD A 401 source : AC1 5) chain A residue 299 type sequence T description binding site for residue DMS A 402 source : AC2 6) chain A residue 300 type sequence T description binding site for residue DMS A 402 source : AC2 7) chain A residue 301 type sequence D description binding site for residue DMS A 402 source : AC2 8) chain A residue 310 type sequence V description binding site for residue DMS A 402 source : AC2 9) chain A residue 334 type sequence E description binding site for residue DMS A 402 source : AC2 10) chain A residue 89 type sequence L description binding site for residue DMS A 403 source : AC3 11) chain A residue 90 type sequence N description binding site for residue DMS A 403 source : AC3 12) chain A residue 93 type sequence R description binding site for residue DMS A 403 source : AC3 13) chain A residue 349 type sequence E description binding site for residue DMS A 403 source : AC3 14) chain A residue 18 type sequence F description binding site for residue DMS A 404 source : AC4 15) chain A residue 86 type sequence E description binding site for residue DMS A 405 source : AC5 16) chain A residue 136 type sequence G description binding site for residue DMS A 405 source : AC5 17) chain A residue 233 type sequence A description binding site for residue DMS A 405 source : AC5 18) chain A residue 235 type sequence Y description binding site for residue DMS A 405 source : AC5 19) chain A residue 129 type sequence F description binding site for residue DAR A 406 source : AC6 20) chain A residue 133 type sequence R description binding site for residue DAR A 406 source : AC6 21) chain A residue 169 type sequence P description binding site for residue DAR A 406 source : AC6 22) chain A residue 170 type sequence E description binding site for residue DAR A 406 source : AC6 23) chain A residue 192 type sequence K description binding site for residue DAR A 406 source : AC6 24) chain A residue 230 type sequence E description binding site for residue DAR A 406 source : AC6 25) chain A residue 166 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 49 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 72 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 139 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 49-72 type prosite sequence LGTGSFGRVMLVKHKETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK source prosite : PS00107 34) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 35) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI7 36) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI8 37) chain A residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI9

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