eF-site ID 1cmk-E PDB Code 1cmk Chain E click to enlarge Title CRYSTAL STRUCTURES OF THE MYRISTYLATED CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE REVEAL OPEN AND CLOSED CONFORMATIONS Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound cAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT Source Bos taurus (Bovine) (IPKA_HUMAN) Sequence E:  GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHL DQFERIKTLGTGSFGRVMLVKHKETGNHFAMKILDKQKVV KLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVM EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSL DLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWXLCG TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR FGNLKDGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKG PGDTSNFDDYEEEEIRVXINEKCGKEFSEF Description (1)  CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) Functional site 1) chain E residue 1 type sequence G description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 2) chain E residue 14 type sequence S description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 3) chain E residue 18 type sequence F description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 4) chain E residue 100 type sequence F description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 5) chain E residue 152 type sequence L description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 6) chain E residue 156 type sequence Y description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 7) chain E residue 303 type sequence I description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 8) chain E residue 306 type sequence Y description BINDING SITE FOR RESIDUE MYR E 0 source : AC3 9) chain E residue 51 type sequence T description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 10) chain E residue 84 type sequence Q description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 11) chain E residue 87 type sequence H description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 12) chain E residue 127 type sequence E description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 13) chain E residue 129 type sequence F description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 14) chain E residue 133 type sequence R description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 15) chain E residue 168 type sequence K description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 16) chain E residue 169 type sequence P description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 17) chain E residue 170 type sequence E description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 18) chain E residue 187 type sequence F description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 19) chain E residue 197 type sequence X description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 20) chain E residue 198 type sequence L description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 21) chain E residue 199 type sequence C description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 22) chain E residue 200 type sequence G description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 23) chain E residue 201 type sequence T description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 24) chain E residue 202 type sequence P description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 25) chain E residue 203 type sequence E description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 26) chain E residue 204 type sequence Y description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 27) chain E residue 230 type sequence E description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 28) chain E residue 235 type sequence Y description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 29) chain E residue 239 type sequence F description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 30) chain E residue 240 type sequence A description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 31) chain E residue 241 type sequence D description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 32) chain E residue 241 type sequence D description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 33) chain E residue 246 type sequence I description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 34) chain E residue 247 type sequence Y description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 35) chain E residue 321 type sequence P description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 36) chain E residue 322 type sequence G description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 37) chain E residue 326 type sequence N description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 38) chain E residue 327 type sequence F description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 39) chain E residue 328 type sequence D description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 40) chain E residue 329 type sequence D description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 41) chain E residue 330 type sequence Y description BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM source : AC4 42) chain E residue 50 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 43) chain E residue 73 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 44) chain E residue 49 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 45) chain E residue 72 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 46) chain E residue 339 type MOD_RES sequence I description Phosphoserine => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI10 47) chain E residue 122 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 48) chain E residue 169 type BINDING sequence P description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 49) chain E residue 121 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 50) chain E residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 51) chain E residue 3 type MOD_RES sequence A description Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123 source Swiss-Prot : SWS_FT_FI4 52) chain E residue 11 type MOD_RES sequence E description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI5 53) chain E residue 10 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI5 54) chain E residue 49 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 55) chain E residue 196 type MOD_RES sequence W description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 56) chain E residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 57) chain E residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 58) chain E residue 140 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI7 59) chain E residue 139 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI7 60) chain E residue 198 type MOD_RES sequence L description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI8 61) chain E residue 331 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI9 62) chain E residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI9 63) chain E residue 167 type catalytic sequence L description 757 source MCSA : MCSA1 64) chain E residue 169 type catalytic sequence P description 757 source MCSA : MCSA1 65) chain E residue 172 type catalytic sequence L description 757 source MCSA : MCSA1 66) chain E residue 185 type catalytic sequence F description 757 source MCSA : MCSA1 67) chain E residue 202 type catalytic sequence P description 757 source MCSA : MCSA1 68) chain E residue 2 type LIPID sequence N description N-myristoyl glycine => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI11 69) chain E 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_FI12 70) chain E residue 2 type MOD_RES sequence N description Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:9521123 source Swiss-Prot : SWS_FT_FI13 71) chain E residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI14 72) chain E residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI15 73) chain E residue 1 type LIPID sequence G description N-myristoyl glycine => ECO:0000269|PubMed:9521123 source Swiss-Prot : SWS_FT_FI16 74) chain E residue 49-72 type prosite sequence LGTGSFGRVMLVKHKETGNHFAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........FAMK source prosite : PS00107 75) chain E residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108

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